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Copper complexes of (−)‐epicatechin gallate and (−)‐epigallocatechin gallate act as inhibitors of Ribonuclease A
Author(s) -
Ghosh Kalyan Sundar,
Maiti Tushar Kanti,
Mandal Abhishek,
Dasgupta Swagata
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.07.054
Subject(s) - gallate , chemistry , epigallocatechin gallate , polyphenol , rnase p , ribonuclease , agarose gel electrophoresis , propyl gallate , copper , epicatechin gallate , circular dichroism , gel electrophoresis , agarose , enzyme , biochemistry , copper protein , nuclear chemistry , organic chemistry , dna , antioxidant , rna , gene
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.