Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers

Horne WS; Johnson LM; Ketas TJKlasse PJLu MMoore JPGellman SH

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Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers

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Unnatural oligomers that can mimic protein surfaces offer a potentially useful strategy for blocking biomedically important protein-protein interactions. Here we evaluate an approach based on combining alpha- and beta-amino acid residues in the context of a polypeptide sequence from the HIV protein gp41, which represents an excellent testbed because of the wealth of available structural and biological information. We show that alpha/beta-peptides can mimic structural and functional properties of a critical gp41 subunit. Physical studies in solution, crystallographic data, and results from cell-fusion and virus-infectivity assays collectively indicate that the gp41-mimetic alpha/beta-peptides effectively block HIV-cell fusion via a mechanism comparable to that of gp41-derived alpha-peptides. An optimized alpha/beta-peptide is far less susceptible to proteolytic degradation than is an analogous alpha-peptide. Our findings show how a two-stage design approach, in which sequence-based alpha ->beta replacements are followed by site-specific backbone rigidification, can lead to physical and biological mimicry of a natural biorecognition process.

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《Proceedings of the National Academy of Sciences of the United States of America》 |2009年第35期|14751-14756|共6页
作者
Horne WS; Johnson LM; Ketas TJKlasse PJLu MMoore JPGellman SH;
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作者单位

Cornell Univ, Weill Med Coll, Dept Microbiol & Immunol, New York, NY 10021 USA.;

Cornell Univ, Weill Med Coll, Dept Biochem, New York, NY 10021 USA.;

Univ Wisconsin, Dept Chem, Madison, WI 53706 USA.;

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收录信息美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种英语
中图分类自然科学总论;
关键词
alpha/beta-peptides; HIV; protein folding; protein-protein interactions;

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Structural and biological mimicry of protein surface recognition by alpha/beta-peptide foldamers

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