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Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies.

ABSTRACT: Structure-activity relationship studies were conducted on HIV integrase (IN) inhibitory peptides which were found by the screening of an overlapping peptide library derived from HIV-1 gene products. Since these peptides located in the second helix of Vpr are considered to have an alpha-helical conformation, Glu-Lys pairs were introduced into the i and i+4 positions to increase the helicity of the lead compound possessing an octa-arginyl group. Ala-scan was also performed on the lead compound for the identification of the amino acid residues responsible for the inhibitory activity. The results indicated the importance of an alpha-helical structure for the expression of inhibitory activity, and presented a binding model of integrase and the lead compound.

SUBMITTER: Suzuki S 

PROVIDER: S-EPMC4486254 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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Peptidic HIV integrase inhibitors derived from HIV gene products: structure-activity relationship studies.

Suzuki Shintaro S   Maddali Kasthuraiah K   Hashimoto Chie C   Urano Emiko E   Ohashi Nami N   Tanaka Tomohiro T   Ozaki Taro T   Arai Hiroshi H   Tsutsumi Hiroshi H   Narumi Tetsuo T   Nomura Wataru W   Yamamoto Naoki N   Pommier Yves Y   Komano Jun A JA   Tamamura Hirokazu H  

Bioorganic & medicinal chemistry 20100725 18

Structure-activity relationship studies were conducted on HIV integrase (IN) inhibitory peptides which were found by the screening of an overlapping peptide library derived from HIV-1 gene products. Since these peptides located in the second helix of Vpr are considered to have an alpha-helical conformation, Glu-Lys pairs were introduced into the i and i+4 positions to increase the helicity of the lead compound possessing an octa-arginyl group. Ala-scan was also performed on the lead compound for  ...[more]

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