Isolation of HIV-1 Protease-Inhibiting Peptides from Thermolysin Hydrolysate of Oyster Proteins
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 vario...
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Veröffentlicht in: | Biochemical and biophysical research communications 1998-12, Vol.253 (3), p.604-608 |
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Sprache: | eng |
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Zusammenfassung: | 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 IC50values of 20 and 15 nM, respectively, and behaved as competitive inhibitors for HIV-1 protease withKivalues of 13 and 10 nM, respectively. These peptides were more potent as an HIV-1 protease inhibitor than pepstatin A. |
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ISSN: | 0006-291X 1090-2104 |
DOI: | 10.1006/bbrc.1998.9824 |