| pubmed-article:16173723 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16173723 | lifeskim:mentions | umls-concept:C0019682 | lld:lifeskim |
| pubmed-article:16173723 | lifeskim:mentions | umls-concept:C0019699 | lld:lifeskim |
| pubmed-article:16173723 | lifeskim:mentions | umls-concept:C0332466 | lld:lifeskim |
| pubmed-article:16173723 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:16173723 | pubmed:issue | 38 | lld:pubmed |
| pubmed-article:16173723 | pubmed:dateCreated | 2005-9-21 | lld:pubmed |
| pubmed-article:16173723 | pubmed: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. | lld:pubmed |
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| pubmed-article:16173723 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16173723 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16173723 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16173723 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16173723 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16173723 | pubmed:issn | 0002-7863 | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:SchepartzAlan... | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:HodsdonMichae... | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:WelchBrett... | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:StephensOlen... | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:KayMichael... | lld:pubmed |
| pubmed-article:16173723 | pubmed:author | pubmed-author:KimSunghwanS | lld:pubmed |
| pubmed-article:16173723 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16173723 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:16173723 | pubmed:volume | 127 | lld:pubmed |
| pubmed-article:16173723 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16173723 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16173723 | pubmed:pagination | 13126-7 | lld:pubmed |
| pubmed-article:16173723 | pubmed:dateRevised | 2011-6-16 | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:meshHeading | pubmed-meshheading:16173723... | lld:pubmed |
| pubmed-article:16173723 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16173723 | pubmed:articleTitle | Inhibiting HIV fusion with a beta-peptide foldamer. | lld:pubmed |
| pubmed-article:16173723 | pubmed:affiliation | Department of Chemistry, , Yale University, New Haven, Connecticut 06520-8107, USA. | lld:pubmed |
| pubmed-article:16173723 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16173723 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16173723 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16173723 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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