Remodeling of gp41-C34 Peptide Leads to Highly Effective Inhibitors of the Fusion of HIV-1 with Target Cells We thank Dr. Terrence R. Burke, Jr., NCI, NIH, Frederick, MD 21702-1201, for proofreading the manuscript and providing useful comments. This research was supported in part by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology, Japan, the Japan Society for the Promotion of Science, and the Japan Health Science Foundation.

Abstract

Substitution in the outer surface of the six-helix peptide bundle improved the solubility and enhanced the anti-HIV-1 activity of SC peptides. The E and K residues at positions b, c, f, and g (see scheme) stabilize the α-helix conformation critical to inhibition; the Z residues at positions a, d, and e interact with the inner strand.