Journal
BIOORGANIC & MEDICINAL CHEMISTRY
Volume 16, Issue 20, Pages 9184-9187Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.bmc.2008.09.018
Keywords
HIV-1; fusion inhibitor; alpha-helix; heptad repeat
Funding
- Ministry of Health and Welfare and the Ministry of Education, Culture, Sports, Science, and Technology of Japan
- The Japan Health Sciences Foundation
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Emergence of multi-drug resistant HIV-1 is a serious problem for AIDS treatment. Recently, the virus-cell membrane fusion process has been identified as a promising target for the development of novel drugs against these resistant variants. In this study, we identified a 29-residue peptide fusion inhibitor, SC29EK, which shows activity comparable to the previously reported inhibitor SC35EK. Some residues in SC29EK not required for interaction with virus gp41 heptad repeat 1 (HR1) were replaced with a non-proteinogenic amino acid, 2-aminoisobutyric acid (Aib), to stabilize the alpha-helix structure and to provide resistance to peptidases. (C) 2008 Elsevier Ltd. All rights reserved.
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