Inhibiting HIV fusion with a beta-peptide foldamer.
Identifieur interne : 002534 ( PubMed/Curation ); précédent : 002533; suivant : 002535Inhibiting HIV fusion with a beta-peptide foldamer.
Auteurs : Olen M. Stephens [États-Unis] ; Sunghwan Kim ; Brett D. Welch ; Michael E. Hodsdon ; Michael S. Kay ; Alanna SchepartzSource :
- Journal of the American Chemical Society [ 0002-7863 ] ; 2005.
Descripteurs français
- KwdFr :
- MESH :
- pharmacologie : Inhibiteurs de fusion du VIH, Oligopeptides.
- synthèse chimique : Oligopeptides.
- Cellules HeLa, Fusion cellulaire, Humains, Inhibiteurs de fusion du VIH, Oligopeptides, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
English descriptors
- KwdEn :
- MESH :
- chemical , chemical synthesis : Oligopeptides.
- chemical , chemistry : HIV Fusion Inhibitors, Oligopeptides.
- chemical , pharmacology : HIV Fusion Inhibitors, Oligopeptides.
- drug effects : HIV-1.
- Cell Fusion, HeLa Cells, Humans.
Abstract
Linear peptides derived from the HIV gp41 C-terminus (C-peptides), such as the 36-residue Fuzeon, are potent HIV fusion inhibitors. These molecules bind to the N-peptide region of gp41 and inhibit an intramolecular protein-protein interaction that powers fusion of the viral and host cell membranes. The N-peptide region contains a surface pocket that is occupied in the post-fusion state by three alpha-helical residues found near the gp41 C-terminus: Trp628, Trp631, and Ile635-the WWI epitope. Here, we describe a set of beta3-decapeptides (betaWWI-1-4) in which the WWI epitope is presented on one face of a short 14-helix stabilized by macrodipole neutralization and side chain-side chain salt bridges. betaWWI-1-4 bind in vitro to IZN17, a validated gp41 model, and inhibit syncytia formation in cell culture. Molecules lacking a complete WWI functional epitope neither bind IZN17 nor inhibit syncytia formation. These results provide evidence that short beta-peptide 14-helices can inhibit an intramolecular protein-protein interaction in vivo. Molecules related to betaWWI-1-4 could represent starting points for the development of highly potent inhibitors or antigens effective against HIV or other viruses, including SARS, Ebola, HRSV, and influenza, that employ common fusion mechanisms.
DOI: 10.1021/ja053444+
PubMed: 16173723
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Stephens</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, , Yale University, New Haven, Connecticut 06520-8107, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, , Yale University, New Haven, Connecticut 06520-8107</wicri:regionArea></affiliation></author><author><name sortKey="Kim, Sunghwan" sort="Kim, Sunghwan" uniqKey="Kim S" first="Sunghwan" last="Kim">Sunghwan Kim</name></author><author><name sortKey="Welch, Brett D" sort="Welch, Brett D" uniqKey="Welch B" first="Brett D" last="Welch">Brett D. Welch</name></author><author><name sortKey="Hodsdon, Michael E" sort="Hodsdon, Michael E" uniqKey="Hodsdon M" first="Michael E" last="Hodsdon">Michael E. Hodsdon</name></author><author><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S" last="Kay">Michael S. Kay</name></author><author><name sortKey="Schepartz, Alanna" sort="Schepartz, Alanna" uniqKey="Schepartz A" first="Alanna" last="Schepartz">Alanna Schepartz</name></author></analytic><series><title level="j">Journal of the American Chemical Society</title><idno type="ISSN">0002-7863</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Fusion</term><term>HIV Fusion Inhibitors (chemistry)</term><term>HIV Fusion Inhibitors (pharmacology)</term><term>HIV-1 (drug effects)</term><term>HeLa Cells</term><term>Humans</term><term>Oligopeptides (chemical synthesis)</term><term>Oligopeptides (chemistry)</term><term>Oligopeptides (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa</term><term>Fusion cellulaire</term><term>Humains</term><term>Inhibiteurs de fusion du VIH ()</term><term>Inhibiteurs de fusion du VIH (pharmacologie)</term><term>Oligopeptides ()</term><term>Oligopeptides (pharmacologie)</term><term>Oligopeptides (synthèse chimique)</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) ()</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>HIV Fusion Inhibitors</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>HIV Fusion Inhibitors</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>HIV-1</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Inhibiteurs de fusion du VIH</term><term>Oligopeptides</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Oligopeptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Fusion</term><term>HeLa Cells</term><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cellules HeLa</term><term>Fusion cellulaire</term><term>Humains</term><term>Inhibiteurs de fusion du VIH</term><term>Oligopeptides</term><term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Linear peptides derived from the HIV gp41 C-terminus (C-peptides), such as the 36-residue Fuzeon, are potent HIV fusion inhibitors. These molecules bind to the N-peptide region of gp41 and inhibit an intramolecular protein-protein interaction that powers fusion of the viral and host cell membranes. The N-peptide region contains a surface pocket that is occupied in the post-fusion state by three alpha-helical residues found near the gp41 C-terminus: Trp628, Trp631, and Ile635-the WWI epitope. Here, we describe a set of beta3-decapeptides (betaWWI-1-4) in which the WWI epitope is presented on one face of a short 14-helix stabilized by macrodipole neutralization and side chain-side chain salt bridges. betaWWI-1-4 bind in vitro to IZN17, a validated gp41 model, and inhibit syncytia formation in cell culture. Molecules lacking a complete WWI functional epitope neither bind IZN17 nor inhibit syncytia formation. These results provide evidence that short beta-peptide 14-helices can inhibit an intramolecular protein-protein interaction in vivo. Molecules related to betaWWI-1-4 could represent starting points for the development of highly potent inhibitors or antigens effective against HIV or other viruses, including SARS, Ebola, HRSV, and influenza, that employ common fusion mechanisms.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16173723</PMID><DateCompleted><Year>2005</Year><Month>12</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0002-7863</ISSN><JournalIssue CitedMedium="Print"><Volume>127</Volume><Issue>38</Issue><PubDate><Year>2005</Year><Month>Sep</Month><Day>28</Day></PubDate></JournalIssue><Title>Journal of the American Chemical Society</Title><ISOAbbreviation>J. Am. Chem. Soc.</ISOAbbreviation></Journal><ArticleTitle>Inhibiting HIV fusion with a beta-peptide foldamer.</ArticleTitle><Pagination><MedlinePgn>13126-7</MedlinePgn></Pagination><Abstract><AbstractText>Linear peptides derived from the HIV gp41 C-terminus (C-peptides), such as the 36-residue Fuzeon, are potent HIV fusion inhibitors. These molecules bind to the N-peptide region of gp41 and inhibit an intramolecular protein-protein interaction that powers fusion of the viral and host cell membranes. The N-peptide region contains a surface pocket that is occupied in the post-fusion state by three alpha-helical residues found near the gp41 C-terminus: Trp628, Trp631, and Ile635-the WWI epitope. Here, we describe a set of beta3-decapeptides (betaWWI-1-4) in which the WWI epitope is presented on one face of a short 14-helix stabilized by macrodipole neutralization and side chain-side chain salt bridges. betaWWI-1-4 bind in vitro to IZN17, a validated gp41 model, and inhibit syncytia formation in cell culture. Molecules lacking a complete WWI functional epitope neither bind IZN17 nor inhibit syncytia formation. These results provide evidence that short beta-peptide 14-helices can inhibit an intramolecular protein-protein interaction in vivo. Molecules related to betaWWI-1-4 could represent starting points for the development of highly potent inhibitors or antigens effective against HIV or other viruses, including SARS, Ebola, HRSV, and influenza, that employ common fusion mechanisms.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stephens</LastName><ForeName>Olen M</ForeName><Initials>OM</Initials><AffiliationInfo><Affiliation>Department of Chemistry, , Yale University, New Haven, Connecticut 06520-8107, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kim</LastName><ForeName>Sunghwan</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Welch</LastName><ForeName>Brett D</ForeName><Initials>BD</Initials></Author><Author ValidYN="Y"><LastName>Hodsdon</LastName><ForeName>Michael E</ForeName><Initials>ME</Initials></Author><Author ValidYN="Y"><LastName>Kay</LastName><ForeName>Michael S</ForeName><Initials>MS</Initials></Author><Author 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