Premium
Surface‐enhanced Raman spectroscopy study of the interaction of the antitumoral drug emodin with human serum albumin
Author(s) -
Fabriciova G.,
SanchezCortes S.,
GarciaRamos J. V.,
Miskovsky P.
Publication year - 2004
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.20058
Subject(s) - chemistry , human serum albumin , binding site , albumin , drug , serum albumin , plasma protein binding , emodin , fatty acid , biochemistry , stereochemistry , pharmacology , medicine
Surface‐enhanced Raman spectroscopy was employed in this work to study the interaction between the antitumoral drug emodin and human serum albumin (HSA), as well as the influence of fatty acids in this interaction. We demonstrated that the drug/protein interaction can take place through two different binding sites which are probably localized in the IIA and IIIA hydrophobic pockets of HSA and which correspond to Sudlow's I and II binding sites, respectively. The primary interaction site of this drug seems to be site II in the defatted albumin. Fatty acids seem to displace the drug from site II to site I in nondefatted HSA, due to the high affinity of fatty acids for site II. The drug interacts with the protein through its dianionic form in defatted HSA (when placed in the site II) and through its neutral form in the site I of nondefatted albumins. © 2004 Wiley Periodicals, Inc. Biopolymers, 2004