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Copper complexes of (-)-epicatechin gallate and (-)-epigallocatechin gallate act as inhibitors of Ribonuclease A
Authors:Ghosh Kalyan Sundar  Maiti Tushar Kanti  Mandal Abhishek  Dasgupta Swagata
Affiliation:Department of Chemistry, Indian Institute of Technology, Kharagpur 721302, India.
Abstract:Green tea polyphenols, which have the ability to inhibit angiogenesis, form complexes with Cu(II), a known potent stimulator of blood vessel proliferation. Copper complexes of (-)-epicatechin gallate and (-)-epigallocatechin gallate were found to inhibit the enzymatic activity of Ribonuclease A (RNase A) as revealed by an agarose gel based assay and urea denatured gel electrophoresis. The copper complexes were found to be non-competitive inhibitors of RNase A with inhibition constants in the micromolar range. Changes in the secondary structure of the protein are found to occur due to the interaction as revealed from Fourier transform infrared and circular dichroism studies.
Keywords:RNase A, Ribonuclease A   ECG, (−)-epicatechin gallate   EGCG, (−)-epigallocatechin gallate   HSA, human serum albumin   2′,3′-cCMP, Cytidine 2′,3′ cyclic monophosphate   tRNA, transfer ribonucleic acid   Mes, 4-morpholine ethanesulphonic acid   FT-IR, Fourier transformed infrared   CD, circular dichroism
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