Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin英文文献资料.docVIP

Vol.2, No.6, 563-570 (2010) Natural Science /10.4236/ns.2010.26071 Binding of naturally occurring hydroxycinnamic acids to bovine serum albumin Lucie Trnková , Iva Bou?ová , Vladimír Kubí?ek , Jaroslav Dr?ata 1,2 1* 1 1,2 1 2 Charles University in Prague, Faculty of Pharmacy, Hradec Králové, Czech Republic; *Corresponding Author: Iva.Bousova@faf.cuni.cz University of Hradec Králové, Faculty of Education, Hradec Králové, Czech Republic Received 22 February 2010; revised 12 April 2010; accepted 13 May 2010. ABSTRACT play crucial role in promoting research on proteins be- cause they can provide useful information for study of pharmacological and biological effects of drugs as well as conformational changes of proteins caused by drugs. Serum albumin is one of the most abundant proteins in circulatory system of a wide variety of organisms and one of the most extensively studied proteins at all [4,5]. Bovine serum albumin (BSA) consists of 583 amino acids in a single polypeptide chain cross-linked with 17 disulfide bonds. It is composed of three homologous domains (I-III), each of which comprises of two subdo- mains (A and B). BSA has two tryptophan residues, which significantly contribute to the intrinsic fluores- cence of this protein: Trp-134 is located near the surface in domain IB and Trp-212 is buried in a hydrophobic (non-polar) pocket in the internal part of domain IIA [6]. HSA differs from BSA by 24% of primary structure and the most important difference from spectroscopic point of view seems to be presence of only one tryptophan residue (Trp-214) in its molecule [4,5]. Serum albumin possesses a wide range of physiological functions in- volving the binding, transport and deposition of many endogenous and exogenous ligands present in blood