Design, synthesis and structure-activity study of shorter hexa peptide analogues as HIV-1 protease inhibitors.
Inhibition of HIV-1 protease enzyme can render the Human Immunodeficiency Virus (HIV-1) non-infectious in vitro. Previous studies have shown that several shorter peptides were discovered as HIV-1 protease inhibitors. In this context, a series of shorter synthetic hexapeptides, Leu-Leu-Glu-Tyr-Val-Xaa (Xaa=Phe, Met, Tyr and Trp), were designed. The synthesized hexa peptides were screened for their HIV-1 protease inhibition. These peptides showed moderately good HIV-1 protease inhibition when compared to acetyl pepstatin.
Narendra Babu
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Department of Studies in Chemistry, University of Mysore, Manasagangotri, Mysore 570006, Karnataka, India.
Rangappa
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D000595:Amino Acid Sequence; D000818:Animals; D020650:Combinatorial Chemistry Techniques; D015195:Drug Design; D017320:HIV Protease Inhibitors / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology; D015497:HIV-1 / Q000187:drug effects*; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000494:pharmacology*; D049895:Ostrea / Q000737:chemistry*; D010436:Pepstatins / Q000494:pharmacology; D013329:Structure-Activity Relationship; D013820:Thermolysin / Q000378:metabolism
D017320:HIV Protease Inhibitors; D009842:Oligopeptides; D010436:Pepstatins; C014195:Streptomyces pepsin inhibitor; D013820:Thermolysin