We have recently shown that alpha-MAPI, a peptidic aldehyde of microbial origin, inhibits the HIV protease with a potency comparable to pepstatin, having, differently from pepstatin, no activity on other aspartic proteases. In this study different peptide derivatives containing a C-terminal aldehyde have been tested to assess the potential of this function for the inhibition of HIV protease. The results of our analysis correspond with the recently published subsite preferences of the viral enzyme, indicating that aldehydes bind to the active site of the HIV protease. Our data suggest that peptide aldehydes can act in their hydrated forms as transition state analogues with the most potent inhibitor having an IC50 of 0.9 microM.

Peptide aldehydes as inhibitors of HIV protease / E. Sarubbi, P. Seneci, M.R. Angelastro, N.P. Peet, M. Denaro, K. Islam. - In: FEBS LETTERS. - ISSN 0014-5793. - 319:3(1993 Mar 22), pp. 253-256.

Peptide aldehydes as inhibitors of HIV protease

P. Seneci
Secondo
;
1993

Abstract

We have recently shown that alpha-MAPI, a peptidic aldehyde of microbial origin, inhibits the HIV protease with a potency comparable to pepstatin, having, differently from pepstatin, no activity on other aspartic proteases. In this study different peptide derivatives containing a C-terminal aldehyde have been tested to assess the potential of this function for the inhibition of HIV protease. The results of our analysis correspond with the recently published subsite preferences of the viral enzyme, indicating that aldehydes bind to the active site of the HIV protease. Our data suggest that peptide aldehydes can act in their hydrated forms as transition state analogues with the most potent inhibitor having an IC50 of 0.9 microM.
Aspartic protease; Human immunodeficiency virus; Microbial alkaline protease inhibitor; Peptide aldehyde; Transition state analogue
Settore CHIM/06 - Chimica Organica
22-mar-1993
Article (author)
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/170324
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