Effective blocking of HIV‐1 proteinase activity by characteristic inhibitors of aspartic proteinases

FEBS Letters

Dunn, Ben M.³  Graves, Mary C.¹  Roberts, Ray³  Richards, Anthony D.²  Kay, John² 

[1] Department of Molecular Genetics, Roche Research Center, Hoffmann La Roche Inc., Nutley, NJ 07110, USA;Department of Biochemistry, University of Wales College of Cardiff, PO Box 903, Cardiff CF1 1ST, Wales, USA;Department of Biochemistry & Molecular Biology, J. Hillis Miller Health Centre, Box J-245, University of Florida, Gainesville, FL 32610 USA

关键词: HIV-1 proteinase;    Tight-binding inhibitor;    Acetyl-pepstatin;    Buffer effect;    Ψ[CHOH−CH2];    the hydroxy ethyl peptide bond replacement;    see (1985) J. Biol. Chem. 260;    14–42;   

DOI  :  10.1016/0014-5793(89)81251-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Inhibitory constants (K _i) between 5 and 35 nM were derived (under different conditions of pH and ionic strength) for the interaction of HIV-1 proteinase with acetyl-pepstatin and H-261, two characteristic inhibitors of aspartic proteinases. Thus this enzyme, essential for replication of the AIDS virus, may be classified unequivocally as belonging to this proteinase family.

【 授权许可】

Unknown