A systematic evaluation of the inhibition of HIV-1 protease by its C- and N-terminal peptides

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Abstract

C- and N-terminal peptides of varying lengths corresponding to the dimerization interface of the retroviral protease of the human immunodeficiency virus-1 (HIV-1 protease) have been synthesized and evaluated as inhibitors of HIV-1 protease activity.

C- and N-terminal peptides of varying lengths corresponding to the dimerization interface of the retroviral protease of the human immunodeficiency virus-1 (HIV-1 protease) have been synthesized and evaluated as inhibitors of HIV-1 protease activity.

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    In both cases, the interface region which displays large hydrophobic pockets (Fig. 3B) may be more accessible to ANS. Lipopeptides are the best of known dimerization inhibitors when compared to cross-linked interface peptides (Kid=220 nM [12,13], 780 nM [19]) and conformationally constrained hairpins (Kid=560 nM [15], 5400 nM [16]). This study shows that: (i) the further amino acid elongation of the Pam-tripeptides is not necessary to enhance dimerization inhibitory efficiency; (ii) the binding pocket for the third C-terminal amino acid in 3-mer lipopeptides is hydrophobic and large enough to accommodate a variety of groups, confirming computer design [10,27].

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