Denaturation studies on bovine serum albumin–bile salt system:Bile salt stabilizes bovine serum albumin through hydrophobicity

作     者：Karpagaraj Malarkani Ivy Sarkar Susithra Selvama 

作者机构：Department of ChemistryVel Tech UniversityAvadiChennai 600062India Department of ChemistryIndian Institute of Technology MadrasChennai 600036India Department of ChemistryPSG College of TechnologyPeelameduCoimbatore 641004India 

出 版 物：《Journal of Pharmaceutical Analysis》 (药物分析学报（英文版）)

年 卷 期：2018年第8卷第1期

页      面：27-36页

核心收录：

学科分类：0710[理学-生物学] 1007[医学-药学(可授医学、理学学位)] 1002[医学-临床医学] 0817[工学-化学工程与技术] 0703[理学-化学] 0702[理学-物理学] 10[医学] 

基　　金：DSTSERB India(SB/FT/CS-032/2012) for the financial support 

主　　题：Bile salts Bovine serum albumin Chemical denaturation Thermal denaturation Tryptophan fluorescence Protein stabilization 

摘      要：Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance,especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize them. The present study aimed at using bile salts(BSs), a group of well-known drug delivery systems, for stabilization of *** serum albumin(BSA) was taken as the model protein, whose association with two BSs, namely sodium cholate(Na C) and sodium deoxycholate(Na DC), was studied. Denaturation studies on the preformed BSA-BS systems were carried out under chemical and physical denaturation conditions. Urea was used as the chemical denaturant and BSA-BS systems were subjected to various temperature conditions to understand the thermal(physical) denaturation. With the denaturation conditions prescribed here,the data obtained is informative on the association of BSA-BS systems to be hydrophobic and this effect of hydrophobicity plays an important role in stabilizing the serum albumin in its native state under both chemical and thermal denaturation.