H. Tamamura et al., A low-molecular-weight inhibitor against the chemokine receptor CXCR4: A strong anti-HIV peptide T140, BIOC BIOP R, 253(3), 1998, pp. 877-882
Citations number
39
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
T22 ([Tyr(5,12), Lys(7)]-polyphemusin II) is an 18-residue peptide amide, w
hich has strong anti-MN activity. T22 inhibits the T cell line-tropic (T-tr
opic) HIV-1 infection through its specific binding to a chemokine receptor
CXCR4, which serves as a coreceptor for the entry of T-tropic HIV-1 strains
. Herein, we report our finding of novel 14-residue CXCR4 inhibitors, T134
and T140, on the basis of the T22 structure. In the assays we examined, T14
0 showed the highest inhibitory activity against HIV-1 entry and the strong
est inhibitory effect on the binding of an anti-CXCR4 monoclonal antibody (
12G5) to CXCR4 among all the CXCR4 inhibitors that have been reported up to
now. (C) 1998 Academic Press.