Patrick Tb Ch17

8/18/2019 Patrick Tb Ch17

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Patrick: An Introduction to Medicinal Chemistry 3e

Chapter 17: Antiviral Agents

Type: matching questionTitle: Chapter 17 - Question 0101) Match the ollo!in" terms and deinitions#Feedback: $he purpose o the capsid is to protect the %iral nucleic acid !hen the %irion mo%es &et!een

host cells#Page reference: ''1a# $he protein coat that contains the nucleic acid o a %irus ( Capsid $he orm a %irus takes outside the host cell ( irionc# $he protein su&units that make up the protein coat o a %irus ( Protomer d# $he assem&ly o %iral nucleic acid !ithin a protein coat ( *ucleocapsid

Type: multiple choice questionTitle: Chapter 17 Question 0+0+) ,hat is meant &y .) ss/*AFeedback: /*A stands or ri&onucleic acid# $he .) indicates that the /*A is identical to the messen"er /*A used to code or %iral proteins# $he letters ss stand or sin"le strand#Page reference: ''1a# in"le stranded deo2yri&onucleic acid that is complementary to the messen"er /*A used to code or%iral proteins# ou&le stranded ri&onucleic acid#4c# in"le stranded ri&onucleic acid that is identical to the messen"er /*A used to code or %iralproteins#d# in"le stranded ri&onucleic acid that is complementary to the messen"er /*A used to code or %iralproteins#

Type: multiple choice questionTitle: Chapter 17 Question 0303) ,hich o the ollo!in" is not treated &y aciclo%ir

Feedback: Aciclo%ir is used a"ainst diseases caused &y the herpes simple2 %irus and the %arcella-5oster %irus# 6oth o these are *A %iruses !hereas 8I is an /*A %irus#

Page reference: '''-''9a# Chickenpo24 8uman immunodeiciency %irusc# Cold soresd# hin"les

Type: multiple choice questionTitle: Chapter 17 Question 0'0') ,hat is the acti%e orm o aciclo%ir

OXFORD H i g h e r E d u c a t i o n ;2ord


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Feedback: $he monophosphate and diphosphate o aciclo%ir are synthesised en route to thetriphosphate &ut it is the triphosphate !hich is the acti%e orm#Page reference: '''-''9a# $he compound itsel $he monophosphatec# $he diphosphate4d# $he triphosphate

Type: multiple choice questionTitle: Chapter 17 Question 0909) ,hat nucleoside is mimicked aciclo%ir

Feedback: Aciclo%ir contains the same nucleic acid &ase "uanine) as deo2y"uanosine &ut has anincomplete su"ar moiety#Page reference: '''-''9a# eo2yadenosine eo2ythymidinec# eo2ycytidine4d# eo2y"uanosine

Type: multiple choice questionTitle: Chapter 17 Question 0=0=) ,hich en5yme is inhi&ited &y aciclo%ir

Feedback: *A polymerase is the en5yme !hich duplicates ne! *A usin" each strand o parent *Aas a template or the construction# $he en5ymes re%erse transcriptase and protease are present in 8I



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!hich is an /*A %irus# $hey are not present in the *A %iruses tar"eted &y aciclo%ir# /*A polymerase ispresent in the lu %irus !hich is an /*A %irus# It is not present in the %iruses tar"eted &y aciclo%ir#Page reference: '''-''94a# *A polymerase /*A polymerasec# /e%erse transcriptase

d# Protease

Type: multiple choice questionTitle: Chapter 17 Question 0707) ,hy is aciclo%ir selecti%e or %irally inected cells

Feedback: Aciclo%ir is phosphorylated &y %iral thymidine kinase to the monophosphate !hich is thentaken on to the acti%e triphosphate &y the action o cellular kinases# Aciclo%ir is a poor su&strate orcellular thymidine kinase and so the dru" is acti%ated more slo!ly in non-inected cells#$here is certainly a selecti%e uptake o aciclo%ir into inected cells &ut the dru" can still enter noninected cells# $he acti%ated orm o aciclo%ir can inhi&it cellular *A polymerase in normal cells#8o!e%er this inhi&ition is !eaker than the inhi&ition o %iral *A polymerase# $he dru" is not rapidlymeta&olised in non inected cells#Page reference: '''-''9a# It cannot enter normal cells#

4 It can only &e acti%ated in the presence o %iral thymidine kinase#c# $he acti%ated orm ails to inhi&it the tar"et in uninected cells#d# It is rapidly meta&olised in normal cells#

Type: multiple choice questionTitle: Chapter 17 Question 0>0>) $he ollo!in" structure is is a prodru" leadin" to one o the ollo!in" compounds# ,hich one

Feedback: $he structure is amciclo%ir !hich is a prodru" or penciclo%ir# esciclo%ir is an analo"ue oaciclo%ir and cidoo%ir is an analo"ue o deo2ycytidine 9-monophosphate#Page reference: ''7-''>4a# Penciclo%ir ?amciclo%ir c# Cidoo%ir d# esciclo%ir

Type: multiple choice questionTitle: Chapter 17 Question 0@



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0@) $he acti%ated orm o aciclo%ir has a second mechanism o action other than en5yme inhi&ition#,hat is itFeedback: ;nce the dru" is acti%ated to the triphosphate deri%ati%e it can &e incorporated into the"ro!in" *A chain# ince the su"ar moiety is incomplete no urther nucleotides can &e added andchain "ro!th stops#Page reference: '''-''=

a# Anta"onism o a receptor 4 Chain terminator or *Ac# Alkylatin" a"ent or *Ad# 6lockin" a carrier protein in the cell mem&rane

Type: matching questionTitle: Chapter 17 - Question 1010) ,hat nucleosides are mimicked &y the ollo!in" structures

Feedback: $he nucleosides that are mimicked can &e determined &y identiyin" the nucleic acid &asethat is present on each dru"# In the case o desciclo%ir the nucleic acid moiety under"oes meta&olico2idation in the &ody such that a car&onyl "roup is introduced# $his results in the ormation o the nucleicacid &ase "uanine#Page reference: ''9-''@ 117a# esciclo%ir ( eo2y"uanosine 1) Penciclo%ir ( eo2y"uanosine +) c# Ido2uridine (

eo2ythymidine 1) d# $riluridine ( eo2ythymidine +) e# idara&ine ( eo2y"uanosine 3)Type: multiple choice questionTitle: Chapter 17 Question 1111) ,hat nucleotide is mimicked &y cidoo%ir

Feedback: Cidoo%ir contains the nucleic acid &ase cytosine# It also has a phosphonomethylene "roupto mimic a monophosphate "roup#Page reference: ''7a# eo2yadenosine monophosphate eo2ythymidine monophosphate4c# eo2ycytidine monophosphated# eo2y"uanosine monophosphate

Type: multiple choice questionTitle: Chapter 17 Question 1+



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1+) ,hat disad%anta"e mi"ht the ollo!in" structure ha%e as an anti%iral a"ent compared to cidoo%ir

Feedback: ince the structure has a phosphate "roup it is suscepti&le to en5ymatic hydrolysis# $heother options are not %alid# $he structure could &e phosphorylated to the acti%e triphosphate i it reachedinected cells &ut most o it !ill "et hydrolysed &eore it does so# $he dru" is no more polar orhydropho&ic than cidoo%ir and so this is not a disad%anta"e either#Page reference: ''7

a# It !ill not &e acti%ated to the acti%e dru"4 It is suscepti&le to hydrolysisc# It is too polar d# It is too hydropho&ic

Type: multiple choice questionTitle: Chapter 17 Question 1313) ,hat sort o nucleic acid is carried &y 8IFeedback: 8I contains t!o identical molecules o sin"le stranded /*A !hich are identical to themessen"er /*A used to code or %iral proteins#Page reference: '90a# .) ss*A ds*A

c# -) ss/*A4d# .) ss/*A

Type: multiple choice questionTitle: Chapter 17 Question 1'1') ,hat is the tar"et or the ollo!in" structure 5ido%udine)

Feedback: $he acti%ated orm o is a re%erse transcriptase inhi&itor#Page reference: '9+-'93a# Inte"rase Protease4c# /e%erse transcriptased# *A polymerase

Type: multiple choice questionTitle: Chapter 17 Question 19



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19) ,hat is the acti%e orm o 5ido%udine

Feedback: ;nce the triphosphate is ormed it can mimic the natural nucleotide &uildin" &locks o *A#$his allo!s it to &e reco"nised &y the tar"et en5yme more readily#

Page reference: '9+-'93a# $he structure itsel $he monophosphatec# $he diphosphate4d# $he triphosphate

Type: multiple choice questionTitle: Chapter 17 Question 1=1=) ,hat nucleoside does 5ido%udine mimic

Feedback: ido%udine contains the nucleic acid &ase thymine and a deo2yri&ose su"ar !here an a5ide

"roup has replaced a hydro2y "roup#Page reference: '9+-'93a# eo2yadenosine4 eo2ythymidinec# eo2ycytidined# eo2y"uanosine

Type: multiple choice questionTitle: Chapter 17 Question 1717) 8o! many protein units make up the 8I protease en5ymeFeedback: $here are t!o identical protein su&units makin" up the protease en5yme# $he proteaseen5yme is symmetrical#Page reference: '9=

a# 14 +



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c# 3d# '

Type: multiple choice questionTitle: Chapter 17 Question 1>1>) $he 8I protease en5yme can catalyse the hydrolysis o a particular peptide &ond that is not

hydrolysed &y mammalian proteases# 6et!een !hich amino acids does this take placeFeedback: $he protease en5yme catalyses the hydrolysis o peptide &onds &et!een proline andphenylalanine !here the *-terminus o proline is linked to the C-terminus o phenylalanine#Page reference: '9=a# Phenylalanine and lysine Proline and lysinec# Phenylalanine and tyrosine4d# Proline and phenylalanine

Type: multiple choice questionTitle: Chapter 17 Question 1@1@) $he ollo!in" structure saBuina%ir) is a protease inhi&itor#

8o! many &indin" su&sites o the protease acti%e site are occupied &y su&stituents o the a&o%estructureFeedback: $he &indin" sites that are occupied are 1-3 and 1-+#Page reference: '=0-'=1a# 1 34c# 9d# 7

Type: multiple choice questionTitle: Chapter 17 Question +0+0) $he ollo!in" structure saBuina%ir) is a protease inhi&itor#

8o! many &indin" su&sites o the protease acti%e site are occupied &y su&stituents o the a&o%estructure



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Feedback: $he &indin" sites that are occupied are 1-3 and 1-+#Page reference: '=0-'=1a# 1 34c# 9d# 7

Type: multiple choice questionTitle: Chapter 17 Question +1+1) ,hich su&stituent is the ideal &indin" "roup or the 1 &indin" pocket o 8I-proteaseFeedback: $he &en5yl "roup is the residue that is present on the amino acid phenylalanine#Page reference: '=1a# Phenyl -Ph) Phenethyl C8+C8+Ph)

4c# 6en5yl -C8+Ph)

d# -C8+C;*8+

Type: multiple choice question

Title: Chapter 17 Question ++++) $he ollo!in" structure ritona%ir) is a protease inhi&itor#

$he structure A77003 &elo!) !as an early compound in the desi"n o ritona%ir# $his contained a diolsho!n in &lue# ;ne o these hydro2yl "roups !as su&seBuently remo%ed# ,hy

Feedback: 6oth hydro2y "roups are in%ol%ed in hydro"en &ondin" interactions &ut one o the hydro2y"roups is more in%ol%ed than the other# /emo%in" one o the ;8 "roups results in less &indin"interactions &ut there is a net "ain in &indin" sta&ility since less ener"y is reBuired to desol%ate onehydro2yl "roup prior to &indin" than ha%in" to desol%ate t!o such "roups#$he hydro2yl "roup that !as remo%ed !as not actin" as a steric shield and !as not causin" themolecule to &ind in an inacti%e mode#Page reference: '=+-'==a# $he "roup that !as remo%ed !as not takin" part in any hydro"en &ondin" interactions !ith the acti%esite# $he hydro2yl "roup that !as remo%ed !as actin" as a steric shield and pre%entin" the molecule rom&indin" properly#4c# /emo%in" the hydro2yl "roup reduced the ener"y penalty associated !ith desol%ation prior to&indin"#d# $he "roup that !as remo%ed !as participatin" in a hydro"en &ondin" interaction that caused themolecule to &ind in an inacti%e mode#

Type: multiple choice questionTitle: Chapter 17 Question +3+3) $he ollo!in" structure ritona%ir) is a protease inhi&itor#



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$he structure A77003 &elo!) !as an early compound in the desi"n o ritona%ir# $he pyridine rin"s in A77003 !ere replaced !ith thia5olyl heterocycles# ,hy

Feedback: $he pyridine rin"s !ere prone to meta&olism leadin" to N -o2ides !hich !ere Buicklye2creted mainly in &ile# $he thia5olyl rin"s !ere less suscepti&le to this orm o meta&olism#Page reference: '=+-'==4a# $he pyridine rin"s !ere suscepti&le to meta&olic o2idation# $he thia5olyl rin"s !ere smaller and decreased the molecular !ei"ht#c# $he nitro"en atoms o the pyridine rin"s could &e protonated and make the dru" too polar#d# $he thia5olyl rin"s itted &etter into &indin" pockets than the pyridine rin"s#

Type: multiple choice questionTitle: Chapter 17 Question +'+') $he ollo!in" structure ritona%ir) is a protease inhi&itor#

eDE

A mutation in the protease en5yme results in resistance to ritona%ir# ,hich mutation takes placeFeedback: $he isopropyl side chain o %aline has an important %an der ,aals interaction !ith an

isopropyl su&stituent on ritona%ir# Alterin" this amino acid eliminates the interaction and results in !eaker &indin" and !eaker acti%ity#Page reference: '==4a# /eplacement o %aline at position >+ !ith alanine threonine or phenylalanine# /eplacement o alanine at position >+ !ith %aline threonine or phenylalanine#c# /eplacement o phenylalanine at position >+ !ith %aline threonine or alanine#d# /eplacement o threonine at position >+ !ith %aline alanine or phenylalanine#

Type: multiple choice questionTitle: Chapter 17 Question +9+9) /itona%ir is a protease inhi&itor#

A mutation in the protease en5yme results in resistance to ritona%ir# An important interaction &et!een the

dru" and the acti%e site is lost as a result o the mutation# ,hich "roup in ritona%ir is in%ol%ed in thisinteraction



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Feedback: $he isopropyl "roup A orms a hydropho&ic interaction !ith the isopropyl side chain presenton %aline#Page reference: '==4a# Froup A Froup 6c# Froup Cd# Froup

Type: multiple choice questionTitle: Chapter 17 Question +=+=) $he ollo!in" structure ritona%ir) is a protease inhi&itor#

$he ollo!in" structure !as de%eloped rom ritona%ir and is acti%e a"ainst %iral strains that are resistant to

ritona%ir# ,hat is it called

Feedback: Gopina%ir is the name o the structure# aBuina%ir !as the irst clinically useul proteaseinhi&itor# Aciclo%ir is not a protease inhi&itor# *elina%ir is a protease inhi&itor &ut it !as not de%elopedrom ritona%ir#Page reference: '=9-'==a# *elina%ir 4 Gopina%ir c# aBuina%ir d# Aciclo%ir

Type: multiple choice questionTitle: Chapter 17 Question +7+7) Gopina%ir is a protease inhi&itor that !as de%eloped rom ritona%ir#

Gopina%ir is acti%e a"ainst %iral strains that are resistant to ritona%ir# ,hat is the si"niicance o the re"ion

sho!n in &lue in lopina%ir



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Feedback: $he rin" imparts conormational restraint on the urea unctional "roup# $his enhances 8-&ondin" interactions &et!een the urea "roup and the + su&site#Page reference: '=9-'==a# It is in%ol%ed in a hydropho&ic interaction !ith the acti%e site#4 It acts as a conormational restraint or the urea "roup#c# It acts as a conormational &locker and orientates the rest o the chain#d# It pre%ents one o the nitro"ens o the urea "roup actin" as a hydro"en &ond donor#


Title: Chapter 17 Question +>+>) ,hat eature o the protease acti%e site permits a hy&ridisation strate"y to &e used in the desi"n oprotease inhi&itorsFeedback: ince the acti%e site is symmetrical inhi&itors can &ind let to ri"ht or ri"ht to let# ince thatis the case it is easi&le to take the ri"ht hand hal o one inhi&itor and link it to the let hand hal o adierent inhi&itor#$he other statements a&o%e are perectly correct &ut do not e2plain !hy the hy&ridisation strate"y iseasi&le# ?or e2ample one option indicates that there are the same num&er o su&sites in either hal &utdoes not indicate that the su&sites in one hal are identical to the correspondin" su&sites in the otherhal#Page reference: '==-'=7a# $here are t!o aspartate residues in the acti%e site !hich are in%ol%ed in the catalytic mechanism othe en5yme#

$here are t!o isoleucine residues in the lap re"ion o the acti%e site#4c# $he acti%e site is symmetrical#d# $here are the same num&er o su&sites in one hal o the acti%e site as the other hal#

Type: multiple choice questionTitle: Chapter 17 Question +@+@) ,hat ad%anta"e is there in replacin" the &en5yl "roup at the P1 position o a protease inhi&itor !itha PhC8+ "roup

Feedback: Incorporatin" a sulphur atom e2tends the side chain allo!in" simultaneous &indin" to the 1and 3 su&sites#Page reference: '=7a# $he ne! "roup its the 1 su&site more eiciently# $he ne! "roup &inds to the 1 and + su&sites simultaneously#

4c# $he ne! "roup &inds to the 1 and 3 su&sites simultaneously#d# $he ne! "roup &inds to the 3 su&site rather than the 1 su&site#

Type: multiple choice questionTitle: Chapter 17 Question 3030) ,hich o the ollo!in" protease inhi&itors incorporates a residue that is capa&le o interactin"simultaneously !ith t!o dierent su&sitesFeedback: *elina%ir has an e2tended P1 residue that can &ind simultaneously to &oth the 1 and 3su&sites#Page reference: '=74a# *elina%ir Palina%ir c# aBuina%ir

d# Amprena%ir



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Type: multiple choice questionTitle: Chapter 17 Question 3131) $he ollo!in" protease inhi&itor palina%ir) illustrates an e2tension strate"y in%ol%in" the "roupsho!n in &lue#

,hich protease inhi&itor does palina%ir mimic on its let hand sideFeedback: $he let hand side or *-terminus side is most closely related to the *-terminus side osaBuina%ir in that &oth structures contain identical P1 and P3 side chains# 8o!e%er the P+ side chain is

dierent and so the molecules are not identical on this sidePage reference: '=>a# *elina%ir Indina%ir 4c# aBuina%ir d# Amprena%ir

Type: multiple choice questionTitle: Chapter 17 Question 3+3+) Amprena%ir is a protease inhi&itor de%eloped &y errt2 Pharmaceuticals# ,hat !as the leadcompound or this structure

Feedback: aBuina%ir !as the lead compound or amprena%ir# $he aim !as to impro%e oral &ioacti%ity&y decreasin" the molecular !ei"ht and peptide character o the structure#Page reference: '=>-'=@a# *elina%ir Palina%ir 4c# aBuina%ir d# Amprena%ir

Type: multiple choice questionTitle: Chapter 17 Question 3333) ,hat sort o nucleic acid is carried &y the lu %irusFeedback: $he lu %irus contains sin"le stranded /*A# It is a ne"ati%e copy !hich means that it iscomplementary to the messen"er /*A used to code or %iral proteins#Page reference: '714a# -)ss/*A .)ss/*Ac# ds/*Ad# ds*A



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Type: multiple choice questionTitle: Chapter 17 Question 3'3') ,hich type o inluen5a %irus is most suscepti&le to mutationsFeedback: Mutations occur almost yearly !ith inluen5a A &ut much more slo!ly !ith inluen5a 6#Mutations do not appear to occur at a si"niicant rate or inluen5a C#Page reference: '73

4a# Inluen5a A Inluen5a 6c# Inluen5a Cd# *one o the ans!ers are correct# $hey are all eBually suscepti&le

Type: multiple choice questionTitle: Chapter 17 Question 3939) Amantadine !as one o the earliest anti%iral dru"s used clinically a"ainst the inluen5a %irus#

,hat is its mechanism o action at lo! concentrationFeedback: At hi"h concentration amantadine acts as a &uer# At lo! concentrations it &locks a %iral ionchannel# It does not &ind to %iral nucleic acid or to a %iral en5yme#

Page reference: '73a# It acts as a &ase and &uers the p8 o endosomes pre%entin" the acidic p8 reBuired or usion totake place &et!een the %iral mem&rane and that o the endosome# It &inds to %iral nucleic acid and pre%ents replication and transcription#4c# It &inds to a speciic re"ion o a %iral ion channel and &locks it#d# It &inds to a %iral en5yme and inhi&its it#

Type: multiple choice questionTitle: Chapter 17 Question 3=3=) Amantadine !as one o the earliest anti%iral dru"s used clinically a"ainst the inluen5a %irus#

,hat is its mechanism o action at hi"h concentration

Feedback: At hi"h concentration amantadine acts as a &uer# At lo! concentrations it &locks a %iral ionchannel# It does not &ind to %iral nucleic acid or to a %iral en5yme#Page reference: '73



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4a# It acts as a &ase and &uers the ph o endosomes pre%entin" the acidic ph reBuired or usion totake place &et!een the %iral mem&rane and that o the endosome# It &inds to %iral nucleic acid and pre%ents replication and transcription#c# It &inds to a speciic re"ion o a %iral ion channel and &locks it#d# It &inds to a %iral en5yme and inhi&its it#

Type: multiple choice questionTitle: Chapter 17 Question 3737) ialic acid &inds to the acti%e site o neuraminidase# ,hich eature o sialic acid has the mostsi"niicant &indin" interaction

Feedback: All the unctional "roups mentioned ha%e a &indin" role &ut the car&o2ylate ion is a&le toorm the stron"est interaction since it is ionic#

Page reference: '7'a# $he triol4 $he car&o2ylate ion

c# $he amided# $he alcohol

Type: multiple choice questionTitle: Chapter 17 Question 3>3>) anami%ir has &een used in the treatment o inluen5a#

,hat is the tar"et or the a&o%e structureFeedback: 8ema""lutinin is a "lycoprotein on the surace o the lu %irus !hich plays a role in theadsorption process# /*A and *A polymerases are en5ymes that catalyse the synthesis o /*A and*A respecti%ely# /*A polymerase is carried &y the lu %irus &ut not *A polymerase# *euraminidase isan en5yme on the surace o the lu %irus that catalyses the splittin" o sialic acid rom "lycoproteins or"lycolipids# $his is the tar"et or 5anami%ir and oseltami%ir#

Page reference: '79-'7>a# 8ema""lutinin



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/*A polymerasec# *A polymerase4d# *euraminidase

Type: multiple choice questionTitle: Chapter 17 Question 3@

3@) anami%ir has &een used in the treatment o inluen5a#

,hat sort o dru" is itFeedback: $he dru" mimics the transition state or the catalytic reaction carried out &y neuraminidase&ut is sta&le to the catalytic process#Page reference: '79-'7>a# Anta"onist Prodru"c# uicide su&strate4d# $ransition state inhi&itor

Type: multiple choice questionTitle: Chapter 17 Question '0

'0) anami%ir has &een used in the treatment o inluen5a#

8o! many &indin" pockets are used &y 5anami%ir !hen it &inds to the tar"et &indin" siteFeedback: $he inhi&itor &inds to the same our &indin" pockets as the natural su&strate#Page reference: '79-'7>a# 1 +c# 34d# '

Type: multiple choice questionTitle: Chapter 17 Question '1'1) anami%ir has &een used in the treatment o inluen5a#



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,hat molecular modellin" sot!are pro"ram !as used in the desi"n o 5anami%irFeedback: F/I !as used to identiy the likely &indin" re"ions !ithin a model acti%e site#Page reference: '79-'7>a# ;CH4 F/Ic# CoM?A

d# Monte-Carlo

Type: multiple choice questionTitle: Chapter 17 Question '+'+) ;seltami%ir is an anti%iral dru" used a"ainst inluen5a#

,hat is the tar"et or oseltami%irFeedback: 8ema""lutinin is a "lycoprotein on the surace o the lu %irus !hich plays a role in theadsorption process# /*A and *A polymerases are en5ymes that catalyse the synthesis o /*A and*A respecti%ely# /*A polymerase is carried &y the lu %irus &ut not *A polymerase# *euraminidase isan en5yme on the surace o the lu %irus that catalyses the splittin" o sialic acid rom "lycoproteins or"lycolipids# $his is the tar"et or 5anami%ir and oseltami%ir

Page reference: '7@-'>1a# 8ema""lutinin /*A polymerase

c# *A polymerase4d# *euraminidase

Type: multiple choice questionTitle: Chapter 17 Question '3'3) ;seltami%ir is an anti%iral dru" used a"ainst inluen5a#



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,hat sort o dru" is itFeedback: $he dru" mimics the transition state or the catalytic reaction carried out &y neuraminidase&ut is sta&le to the catalytic process#Page reference: '7@-'>1a# Anta"onist Prodru"c# uicide su&strate4d# $ransition state inhi&itor

Type: multiple choice questionTitle: Chapter 17 Question '''') $he ollo!in" dru" entered phase III clinical trials or the treatment o the cold %irus#

,hat is it calledFeedback: Pleconaril entered phase III clinical trials or the treatment o the cold %irus# iso2aril alsoentered clinical trials &ut pro%ed too to2ic# anami%ir and oseltami%ir are acti%e a"ainst the lu %irus andnot the cold %irus#Page reference: '>'4a# Pleconaril iso2arilc# anami%ir d# ;seltami%ir

Type: multiple choice questionTitle: Chapter 17 Question '9'9) Pleconaril entered phase III clinical trials or the treatment o the cold %irus#

,hat is the tar"et or pleconarilFeedback: $he tar"et is a protein !hich is a constituent o the %iral protein coat#Page reference: '>3-'>'

a# iral nucleic acid A %iral en5ymec# An anti"en on inected host cells



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4d# A capsid protein

Type: multiple choice questionTitle: Chapter 17 Question '='=) Pleconaril entered phase III clinical trials or the treatment o the cold %irus#

8o! does pleconaril ha%e an anti%iral eectFeedback: $he dru" sta&ilises the %iral protein coat and pre%ents the uncoatin" process#Page reference: '>3-'>'a# It &locks the replication and transcription o %iral nucleic acid

4 It pre%ents the uncoatin" processc# It inhi&its an en5yme catalysed reactiond# It pre%ents adsorption

Type: multiple choice questionTitle: Chapter 17 - Question '7'7) ,hich is the normal order o the ollo!in" e%ents in the lie cycle o %irusesFeedback: $he lie cycle starts !ith the %irus adsor&in" or attachin" to the cell mem&rane o the host cell#Penetration then takes place !ith uncoatin" to ree the %iral nucleic acid# /eplication and transcription leadsto ne! %iral protein allo!in" the assem&ly o nucleocapsids# ?inally the %irus departs the host cell usually&y &uddin"#Page reference: ''1-''+a# Penetration uncoatin" replication and transcription &uddin" assem&ly o nucleopcapsids

6uddin" uncoatin" penetration replication and transcription assem&ly o nucleocapsidsc# ) Match the ollo!in" structures to the anti%iral dru"s &elo!:

Feedback: $he structure is no! kno!n as aciclo%ir# $he old spellin" !as acyclo%ir# alaciclo%ir is an G-%alylprodru" o aciclo%ir# esciclo%ir is an analo"ue o aciclo%ir that lacks a car&onyl "roup#Page reference: '''-''>a# esciclo%ir ( tructure C Aciclo%ir ( tructure A

c# alaciclo%ir ( tructure 6d# Fan"ciclo%ir ( tructure



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Type: matching questionTitle: Chapter 17 - Question '@'@) Match the ollo!in" structures to the anti%iral a"ents:

Feedback: ?amciclo%ir is a prodru" or penciclo%ir# Cidoo%ir is an analo"ue o deo2ycytidine 9-monophosphate# Ido2uridine is an analo"ue o deo2ythymidinePage reference: '''-''>a# Penciclo%ir ( tructure 6 Cidoo%ir ( tructure Cc# Ido2uridine ( tructure d# ?amciclo%ir ( tructure A

Type: multiple choice questionTitle: Chapter 17- Question 9090) ,hich o the ollo!in" statements comparin" cidoo%ir !ith aciclo%ir is trueFeedback: Cidoo%ir is more polar than aciclo%ir due to the phosphonomethylene "roup# As a result it haspoorer oral &ioa%aila&ility# It also has to2ic side eects or the kidneys#$he dru" has the eBui%alent o a monophosphate "roup and so it is acti%e a"ainst %iral strains that lack the%iral thymidine kinase reBuired to acti%ate aciclo%ir and related compounds# $his "i%es cidoo%ir a &roaderspectrum o acti%ity#Page reference: '''-''>4a# It has poorer oral &ioa%aila&ility It is less polar c# It has a narro!er spectrum o acti%ityd# It has e!er side eects

Type: multiple choice questionTitle: Chapter 17- Question 9191) ,hich o the ollo!in" tar"ets is not a current or potential dru" tar"et in anti-8I therapyFeedback: *euraminidase is a dru" tar"et in tacklin" the lu %irus &ut not 8I#Page reference: '90-'9+

a# /e%erse transcriptase Inte"rasec# Protease4d# *euraminidase

Type: multiple choice questionTitle: Chapter 17- Question 9+9+) ,hat role does the en5yme re%erse transcriptase ha%e in the 8I lie cycleFeedback: $he en5yme inte"rase is responsi&le or incorporatin" %iral *A into host *A once it has &eensynthesised# $he en5yme protease is responsi&le or processin" the %iral proteins o 8I ollo!in"transcription and translation# $he en5yme re%erse transcriptase is responsi&le or catalysin" the synthesis o%iral *A rom sin"le stranded /*A once 8I has inected the host cell# $he "lycoprotein "p1+0 alon" !ith"p'1 are crucial to the adsorption and penetration o the %irus#

Page reference: '90-'91a# It catalyses the incorporation o 8I *A into host *A It processes 8I proteins durin" the production o ne! %iruses



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4c# It catalyses the synthesis o 8I *A in the host celld# It is crucial to adsorption and penetration o the %irus

Type: multiple choice questionTitle: Chapter 17- Question 9393) ,hat role does the en5yme inte"rase ha%e in the 8I lie cycle

Feedback: $he en5yme inte"rase is responsi&le or incorporatin" %iral *A into host *A once it has &eensynthesised# $he en5yme protease is responsi&le or processin" the %iral proteins o 8I ollo!in"transcription and translation# $he en5yme re%erse transcriptase is responsi&le or catalysin" the synthesis o%iral *A rom sin"le stranded /*A once 8I has inected the host cell# $he "lycoprotein "p1+0 alon" !ith"p'1 are crucial to the adsorption and penetration o the %irus#Page reference: '90-'914a# It catalyses the incorporation o 8I *A into host *A It processes 8I proteins durin" the production o ne! %irusesc# It catalyses the synthesis o 8I *A in the host celld# It is crucial to adsorption and penetration o the %irus

Type: multiple choice questionTitle: Chapter 17- Question 9'

9') ,hat role does the en5yme protease ha%e in the 8I lie cycleFeedback: $he en5yme inte"rase is responsi&le or incorporatin" %iral *A into host *A once it has &eensynthesised# $he en5yme protease is responsi&le or processin" the %iral proteins o 8I ollo!in"transcription and translation# $he en5yme re%erse transcriptase is responsi&le or catalysin" the synthesis o%iral *A rom sin"le stranded /*A once 8I has inected the host cell# $he "lycoprotein "p1+0 alon" !ith"p'1 are crucial to the adsorption and penetration o the %irus#Page reference: '90-'91a# It catalyses the incorporation o 8I *A into host *A4 It processes 8I proteins durin" the production o ne! %irusesc# It catalyses the synthesis o 8I *A in the host celld# It is crucial to adsorption and penetration o the %irus


Title: Chapter 17- Question 9999) ,hat role does the "lycoprotein "p1+0 ha%e in the 8I lie cycleFeedback: $he en5yme inte"rase is responsi&le or incorporatin" %iral *A into host *A once it has &eensynthesised# $he en5yme protease is responsi&le or processin" the %iral proteins o 8I ollo!in"transcription and translation# $he en5yme re%erse transcriptase is responsi&le or catalysin" the synthesis o%iral *A rom sin"le stranded /*A once 8I has inected the host cell# $he "lycoprotein "p1+0 alon" !ith"p'1 are crucial to the adsorption and penetration o the %irus#Page reference: '90-'91a# It catalyses the incorporation o 8I *A into host *A It processes 8I proteins durin" the production o ne! %irusesc# It catalyses the synthesis o 8I *A in the host cell4d# It is crucial to adsorption and penetration o the %irus

Type: matching questionTitle: Chapter 17 - Question 9=9=) Match the ollo!in" structures !ith the correct dru"s:



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Feedback: All the structures are nucleoside like in that they ha%e a nucleic acid &ase attached to a i%emem&ered rin" !hich mimics a su"ar rin"# All the structures inhi&it the re%erse transcriptase en5yme#Page reference: '9+-'93a# ido%udine ( tructure idanosine ( tructure Cc# ta%udine ( tructure A

d# alcita&ine ( tructure 6

Type: matching questionTitle: Chapter 17 Question 9797) Match the ollo!in" structures to the ollo!in" dru"s

Feedback: All our compounds are e2amples o non-nucleoside re%erse transcriptase inhi&itors#Page reference: '93-'99a# *e%irapine ( tructure C ela%irdine ( tructure c# Ja%iren5 ( tructure 6d# Jmi%irine ( tructure A

Type: multiple choice questionTitle: Chapter 17- Question 9>

9>) ,hich o the ollo!in" statements is true re"ardin" ne%irapine

Feedback: *e%irapine is a chiral molecule that &inds to an allosteric &indin" site ne2t to the acti%e site ore%erse transcriptase# It &ears no resem&lance to a nucleoside and it is a irst "eneration non-nucleosidere%erse transcriptase inhi&itor#



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Page reference: '93-'994a# It is a non nucleoside re%erse transcriptase inhi&itor **/$I)# It &inds to the su&strate &indin" site o re%erse transcriptase#c# It is an achiral molecule#d# It is an e2ample o a second "eneration dru" o its class#

Type: multiple choice questionTitle: Chapter 17- Question 9@9@) ,hich o the ollo!in" statements is true or non-nucleoside re%erse transcriptase inhi&itorsFeedback: $he non-nucleoside re%erse transcriptase inhi&itors &ind to an allosteric &indin" site ne2t to theacti%e site o re%erse transcriptase# ince they do not occupy the acti%e site they can &e used alon"sidenucleoside re%erse transcriptase inhi&itors !hich do occupy the acti%e site# $here are si"niicant &indin"interactions &et!een second and third "eneration **/$Is and the main protein chain in the &indin" site#/esistance can arise due to a mutation !here lysine is mutated to aspara"ine#Page reference: '93-'99a# $hey cannot &e used alon"side nucleoside re%erse transcriptase inhi&itors# $hey &ind to the acti%e site#4c# /esistance can arise due to a mutation !here a lysine in the tar"et &indin" site is mutated to aspara"ine#d# 6indin" interactions &et!een **/$Is and the main protein chain in the &indin" site are not important#

Type: multiple choice questionTitle: Chapter 17- Question =0=0) ,hat role do the aspartate residues Asp +9 and Asp +9 play in the 8I protease en5ymeFeedback: Aspartic acid +9 and +9 are in%ol%ed in the catalytic mechanism !hich hydrolyses the peptide&ond o a protein su&strate#Page reference: '99-'9@a# $hey &ind directly to the su&strate#4 $hey are in%ol%ed in the catalytic mechanism !hich leads to peptide &ond hydrolysis in a proteinsu&strate#c# $hey are located in the lap re"ion o the protease acti%e site and are in%ol%ed in &indin" a !atermolecule# $he latter acts as a hydro"en &ondin" &rid"e to a &ound protein su&strate#d# $hey ha%e no si"niicant role#

Type: multiple choice questionTitle: Chapter 17- Question =1=1) ,hat role do the isoleucine residues Ile 90 and Ile 90 play in the 8I protease en5ymeFeedback: $he amino acids concerned do not &ind directly to the su&strate and are not in%ol%ed directly!ith the mechanism#Page reference: '99-'9@a# $hey &ind directly to the su&strate# $hey are in%ol%ed in the catalytic mechanism !hich leads to peptide &ond hydrolysis in a proteinsu&strate#4c# $hey are located in the lap re"ion o the protease acti%e site and are in%ol%ed in &indin" a !atermolecule# $he latter acts as a hydro"en &ondin" &rid"e to a &ound protein su&strate#d# $hey ha%e no si"niicant role#

Type: multiple choice questionTitle: Chapter 17- Question =+=+) ,hich statement is alseFeedback: ;nly the 8I protease en5yme is symmetrical# ince there is a si"niicant dierence &et!een the8I protease en5yme and mammalian protease en5ymes in terms o symmetry it is easi&le that inhi&itorscould &e desi"ned !hich !ould sho! selecti%ity or the %iral en5yme o%er the mammalian en5ymes#Page reference: '99-'9@4a# 6oth mammalian and 8I protease en5ymes are symmetrical# It is possi&le to desi"n inhi&itors that pro%e selecti%e or the 8I protease o%er mammalian proteases#c# $he protease en5yme o 8I hydrolyses peptide &onds in protein su&strates#d# $he protease en5yme in the 8I en5yme has a dierent su&strate selecti%ity rom protease en5ymes inhumans despite catalysin" the same reaction#

Type: matching question



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Title: Chapter 17 - Question =3=3) Match the ollo!in" structures to the anti%iral a"ents stated &elo!#

Feedback: All these a"ents are protease inhi&itors#Page reference: '9@-'=@a# ritona%ir ( tructure C lopina%ir ( tructure Ac# saBuina%ir ( tructure 6d# indina%ir ( tructure

Type: matching questionTitle: Chapter 17 - Question ='=') $he ollo!in" structure is saBuina%ir# Match the coloured moieties A-J) to the ollo!in" &indin" su&sitesin the 8I protease acti%e site#

Feedback: $he coloured moieties mimic the amino acid residues o protein su&strates that !ould normallyit into these &indin" su&sites#Page reference: '9@-'=1a# su&site 1 ( Moiety J su&site + ( Moiety Cc# su&site 1 ( Moiety 6d# su&site + ( Moiety e# su&site 3 ( Moiety A


Title: Chapter 17- Question =9



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=9) $he ollo!in" structure is saBuina%ir# ,hich coloured moiety orms a hydro"en &ond to Asp+9 and Asp+9 !hen the dru" is &ound to the acti%e site o the 8I protease en5yme

Feedback: $he hydro2y "roup is part o a hydro2yethylamine transition state isostere that mimics a peptide&ond &ut is not hydrolysed#

Page reference: '9@-'=1a# Moiety A Moiety 6c# Moiety C4d# Moiety

Type: multiple choice questionTitle: Chapter 17- Question ====) $he ollo!in" structure is saBuina%ir# ,hich moiety acts as a transition state isostere

Feedback: Moiety is a hydro2yylamine moiety !hich mimics the transition state or the catalytic reaction#It is sta&le to the catalytic reaction#Page reference: '9@-'=1

a# Moiety A Moiety 6c# Moiety C4d# Moiety

Type: matching questionTitle: Chapter 17 - Question =7=7) $he ollo!in" structure is saBuina%ir# Match the ollo!in" "roups to the coloured moieties sho!n A-J)



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Feedback: $he moieties sho!n are desi"ned to it the en5yme &indin" su&sites that !ould normally &eoccupied &y the amino acid residues o protein su&strates#Page reference: '9@-'=1a# Quinoline rin" ( Moiety A ecahydroisoBuinoline rin" ( Moiety Jc# 6en5yl "roup ( Moiety 6d# $ertiary &utyl "roup ( Moiety Ce# Aspara"ine residue ( Moiety

Type: multiple choice questionTitle: Chapter 17- Question =>=>) $he ollo!in" structure is saBuina%ir#

,hich o the ollo!in" structures !as the initial lead compound used in the desi"n o saBuina%ir

Feedback: tructure A is the dipeptide G-phenylalanyl-G-proline# $his dipeptide is hydrolysed &y the 8Iprotease en5yme &ut not &y mammalian protease en5ymes# ince it alredy sho!s selecti%ity inhi&itorsde%eloped rom this su&strate ha%e a "ood chance o sho!in" selecti%ity as !ell#

Page reference: '9@-'=14a# tructure A tructure 6



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c# tructure Cd# tructure

Type: multiple choice questionTitle: Chapter 17- Question =@=@) $he dipeptide G-phenylalanyl-G-proline !as chosen as the lead compound or the de%elopment o

saBuina%ir# ,hich o the ollo!in" statements is the &est e2planation or this choiceFeedback: $he dipeptide !as suscepti&le to hydrolysis# I it had &een sta&le it !ould ha%e &een a poorchoice as a lead compound since it is unlikely that it could &ind eiciently to the acti%e site# As a resultanalo"ues !ould &e unlikely to &ind as !ell# $here is nothin" !ron" !ith the statement the residues o thet!o constituent amino acids it &indin" su&sites in the acti%e site and so analo"ues !ill &e easily reco"nisedand &ound stron"ly# 8o!e%er that !ould not &e a reason in itsel or choosin" this dipeptide# I the dipeptidealso !as &ound stron"ly to mammalian proteases there !ould &e little chance o achie%in" inhi&itorselecti%ity# $he dipeptides o all the naturally occurrin" amino acids are easy to synthesise#Page reference: '9@-'=1a# the dipeptide is sta&le to hydrolysis &y the 8I protease and so any analo"ues are likely to act asinhi&itors rather than su&strates $he residues o the t!o constituent amino acids it &indin" su&sites in the acti%e site and so analo"ues !ill&e easily reco"nised and &ound stron"ly

4c# the 8I protease catalyses the hydrolysis o the dipeptide !hereas mammalian proteases do not# $hisallo!s the possi&ility o tar"et selecti%ity#d# the dipeptide !as easy to synthesise compared to other dipeptides and so su&seBuent analo"ues !ouldalso &e easily o&taina&le

Type: multiple choice questionTitle: Chapter 17- Question 7070) ,hich o the ollo!in" protease inhi&itors !as de%eloped rom a symmetrical lead compoundFeedback: $he early structures leadin" to ritona%ir !ere symmetrical molecules !hich took ad%anta"e othe symmetrical nature o the acti%e site in the 8I protease en5yme#Page reference: '=+-'==4a# /itona%ir *elina%ir

c# aBuina%ir d# Indina%ir

Type: multiple choice questionTitle: Chapter 17- Question 7171) $he lead compound and early structures leadin" to the important protease inhi&itors ritona%ir andlopina%ir !ere symmetrical molecules# ,hy !ere symmetrical molecules chosenFeedback: $hey !ere easy to synthesise and could &ind let to ri"ht or ri"ht to let in the symmetrical&indin" site increasin" the chances o "ood acti%ity &ut these !ere not the principal reasons or choosin"symmetrical lead compounds# $he molecules may ha%e &een symmetrical &ut they still contained chiralcentres#Page reference: '=+-'==a# $hey !ere easy to synthesise#

$hey did not ha%e chiral centres#4c# $he &indin" site or the 8I protease en5yme is symmetrical !hereas the &indin" sites or mammalianproteases are notd# $hey could &ind let to ri"ht or ri"ht to let in the symmetrical &indin" site increasin" the chances o "oodacti%ity#

Type: multiple choice questionTitle: Chapter 17- Question 7+7+) ,hich o the ollo!in" protease inhi&itors !as de%eloped usin" a hy&rid strate"yFeedback: Indina%ir !as de%eloped &y linkin" one hal o a structure containin" a hydro2yethylene transitionstate isostere !ith one hal o saBuina%ir#Page reference: '==-'=7a# /itona%ir

Gopina%ir c# aBuina%ir



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4d# Indina%ir

Type: matching questionTitle: Chapter 17 - Question 7373) Match the ollo!in" structures to the ollo!in" protease inhi&itors

Feedback: All our structures contain a hydro2ylamine transition state isostere in place o the peptide &ond!hich !ould normally &e hydrolysed &y the en5yme#Page reference: '=7-'=@a# *elina%ir ( tructure Palina%ir ( tructure Ac# Ata5ana%ir ( tructure 6d# Amprena%ir ( trcuture C

Type: multiple choice questionTitle: Chapter 17- Question 7'7') Palina%ir is an 8I protease inhi&itor# ,hich o the ollo!in" statements is true re"ardin" the "roupcoloured &lue

Feedback: $he &lue coloured moiety spans t!o &indin" su&sites and does a!ay !ith the need or t!oseparate &indin" "roups# As a result the molecular !ei"ht o the molecule is decreased#Page reference: '=>a# $he moiety in &lue !as added such that !ater solu&ility could &e increased !ith the addition o a pyridine

rin"#4 $he moiety in &lue !as desi"ned to span the t!o &indin" su&sites 1 and 3)#



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c# $he moiety in &lue !as added such that the pyridine rin" could orm a hydro"en &ondin" interaction !ith a&indin" re"ion not normally accessi&le to protein su&strates#d# $he &lue coloured moiety !as added as a steric shield to pre%ent hydrolysis o the C -terminal peptide&ond#


Title: Chapter 17- Question 7979) *euraminidase is an en5yme carried &y the lu %irus# ,hat role does it playFeedback: 8ema""lutinin is a "lycoprotein on the surace o the lu %irus !hich plays a role in theadsorption process# /*A and *A polymerases are en5ymes that catalyse the synthesis o /*A and *Arespecti%ely# *euraminidase is an en5yme that catalyses the splittin" o sialic acid rom "lycoproteins or"lycolipids#Page reference: '71-'73a# It plays a role in the adsorption process It catalyses the synthesis o /*Ac# It catalyses the synthesis o *A4d# It catalyses the splittin" o sialic acid rom "lycoproteins or "lycolipids


Title: Chapter 17- Question 7=7=) 8ema""lutinin is a "lycoprotein carried &y the lu %irus# ,hat role does it playFeedback: 8ema""lutinin is a "lycoprotein on the surace o the lu %irus !hich plays a role in theadsorption process# /*A and *A polymerases are en5ymes that catalyse the synthesis o /*A and *Arespecti%ely# *euraminidase is an en5yme that catalyses the splittin" o sialic acid rom "lycoproteins or"lycolipids#Page reference: '71-'734a# It plays a role in the adsorption process It catalyses the synthesis o /*Ac# It catalyses the synthesis o *Ad# It catalyses the splittin" o sialic acid rom "lycoproteins or "lycolipids


Title: Chapter 17- Question 7777) /*A polymerase is an en5yme carried &y the lu %irus# ,hat role does it playFeedback: 8ema""lutinin is a "lycoprotein on the surace o the lu %irus !hich plays a role in theadsorption process# /*A and *A polymerases are en5ymes that catalyse the synthesis o /*A and *Arespecti%ely# /*A polymerase is carried &y the lu %irus &ut not *A polymerase# *euraminidase is anen5yme on the surace o the lu %irus that catalyses the splittin" o sialic acid rom "lycoproteins or"lycolipids#Page reference: '71-'73a# It plays a role in the adsorption process#4 It catalyses the synthesis o /*A#c# It catalyses the synthesis o *A#d# It catalyses the splittin" o sialic acid rom "lycoproteins or "lycolipids#

Type: matching questionTitle: Chapter 17 - Question 7>7>) $he ollo!in" structures are all used in the treatment o lu# Match the structures a"ainst the ollo!in"dru" names#



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Feedback: Amantadine and rimantadine are e2amples o adamantanes and represent some o the earliestclinically useul anti%iral a"ents# anami%ir and oseltami%ir are more recent dru"s that !ere de%eloped &yrational desi"n as transition state inhi&itors#Page reference: '73-'>1a# anami%ir ( tructure C Amantadine ( tructure

c# /imantadine ( tructure 6d# ;seltami%ir ( tructure A

Type: multiple choice questionTitle: Chapter 17- Question 7@7@) $he ollo!in" structures are all anti%iral a"ents# ,hat %irus are they all used a"ainst

Feedback: ierent %iruses ha%e dierent suscepti&ilities to dru"s# It is important to appreciate that the %irusresponsi&le or colds is dierent rom the %irus responsi&le or lu# As a result dru"s !hich are useul in thetreatment o lu are not useul in the treatment o colds#Page reference: '73-'>+a# 8I4 ?lu %irusc# Cold %irus

d# 8erpes%irus

Type: multiple choice questionTitle: Chapter 17- Question >0>0) ,hich o the ollo!in" statements is untrueFeedback: $he %esicles are called endosomes#Page reference: ''1-''+ '71-'73a# ome %irions are taken into a host cell &y a process kno!n as endocytosis !hich in%ol%es the cellmem&rane !rappin" round the %irion and &ein" pinched o to produce %esicles#4 esicles that ha%e &rou"ht %irions into the host cell are called e2osomes#c# Mem&rane &ound %esicles that contain %irions use !ith cell structures called lysosomes#d# 8ost cell en5ymes can aid the %irus in the uncoatin" process#

Type: multiple choice questionTitle: Chapter 17- Question >1



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>1) ,hich o the ollo!in" statements is alse re"ardin" the characteristics o a "ood protein tar"et oranti%iral dru"sFeedback: $he ideal tar"et should &e shared &et!een %arious %iruses in order to desi"n a dru" !ith a &roadanti%iral acti%ity#Page reference: ''3-'''a# It should &e important to the lie cycle o the %irus#

It should &ear little resem&lance to human proteins#4c# It should &e uniBue or a speciic %irus#d# It should &e important in the early sta"es o the %irus lie cycle#

Type: multiple choice questionTitle: Chapter 17- Question >+>+) Aciclo%ir is a prodru" !hich is phosphorylated in %irally inected cells to the acti%e anti%iral a"ent# ,hicho the ollo!in" structures is the acti%e a"ent

Feedback: It is the triphosphate !hich is the acti%e compound# $he monphosphate and diphosphate are&iosynthetic intermediates to the triphosphate# $he tetraphosphate is not ormed#Page reference: '''-''7a# tructure A tructure 64c# tructure C

d# tructure

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