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Identification of a D-amino acid decapeptide HIV-1 entry inhibitor.

Abstract：

:Entry of human immunodeficiency virus type 1 (HIV-1) virion into host cells involves three major steps, each being a potential target for the development of entry inhibitors: gp120 binding to CD4, gp120-CD4 complex interacting with a coreceptor, and gp41 refolding to form a six-helix bundle. Using a D-amino acid decapeptide combinatorial library, we identified peptide dC13 as having potent HIV-1 fusion inhibitory activity, and effectively inhibiting infection by several laboratory-adapted and primary HIV-1 strains. While dC13 did not block binding of gp120 to CD4, nor disrupt the gp41 six-helix bundle formation, it effectively blocked the binding of an anti-CXCR4 monoclonal antibody and chemokine SDF-1alpha to CXCR4-expressing cells. However, because R5-using primary viruses were also neutralized, the antiviral activity of dC13 implies additional mode(s) of action. These results suggest that dC13 is a useful HIV-1 coreceptor antagonist for CXCR4 and, due to its biostability and simplicity, may be of value for developing a new class of HIV-1 entry inhibitors.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Boggiano C,Jiang S,Lu H,Zhao Q,Liu S,Binley J,Blondelle SE

doi

10.1016/j.bbrc.2006.06.150

subject

Has Abstract

pub_date

2006-09-08 00:00:00

pages

909-15

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(06)01468-9

journal_volume

347

pub_type

杂志文章

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