Abstract Title:

Inhibition of the HIV-1 and HIV-2 proteases by curcumin and curcumin boron complexes.

Abstract Source:

Bioorg Med Chem. 1993 Dec;1(6):415-22. PMID: 8087563

Abstract Author(s):

Z Sui, R Salto, J Li, C Craik, P R Ortiz de Montellano

Article Affiliation:

Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco 94143-0446.


Curcumin, a relatively non-toxic natural product isolated from Curcuma longa, is a modest inhibitor of the HIV-1 (IC50 = 100 microM) and HIV-2 (IC50 = 250 microM) proteases. Simple modifications of the curcumin structure raise the IC50 value but complexes of the central dihydroxy groups of curcumin with boron lower the IC50 to a value as low as 6 microM. The boron complexes are also time-dependent inactivators of the HIV proteases. The increased affinity of the boron complexes may reflect binding of the orthogonal domains of the inhibitor in interesecting sites within the substrate-binding cavity of the enzyme, while activation of the alpha, beta-unsaturated carbonyl group of curcumin by chelation to boron probably accounts for time-dependent inhibition of the enzyme.

Study Type : In Vitro Study

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