Literature DB >> 9918775

Isolation of HIV-1 protease-inhibiting peptides from thermolysin hydrolysate of oyster proteins.

T G Lee1, S Maruyama.   

Abstract

The peptides inhibiting HIV-1 protease were isolated from the hydrolysate of oyster (Crassostrea gigas) proteins prepared with thermolysin. The amino acid sequences of the peptides were determined as Leu-Leu-Glu-Tyr-Ser-Ile and Leu-Leu-Glu-Tyr-Ser-Leu. These sequences exist in some proteins of variola major virus or human cytomegalovirus. Chemically synthesized Leu-Leu-Glu-Tyr-Ser-Ile and Leu-Leu-Glu-Tyr-Ser-Leu showed IC50 values of 20 and 15 nM, respectively, and behaved as competitive inhibitors for HIV-1 protease with Ki values of 13 and 10 nM, respectively. These peptides were more potent as an HIV-1 protease inhibitor than pepstatin A.

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Year:  1998        PMID： 9918775     DOI： 10.1006/bbrc.1998.9824

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN： 0006-291X            Impact factor:   3.575


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