Temperature dependent rapid annealing effect induces amorphous aggregation of human serum albumin.
作者： Mohd Ishtikhar , Mohd. Sajid Ali , Ayman M. Atta , Hammad Al-Lohedan , Gamal Badr
DOI: 10.1016/J.IJBIOMAC.2015.10.071
关键词: Protein aggregation 、 Circular dichroism 、 Rosin 、 Polymer chemistry 、 Serum albumin 、 Chemistry 、 Protein structure 、 Organic chemistry 、 Globular protein 、 Human serum albumin 、 Abietic acid
摘要: This study represents an analysis of the thermal aggregation human serum albumin (HSA) induced by novel rosin modified compounds. The process causes conformational alterations in secondary and tertiary structures proteins. conversion globular protein to amorphous aggregates was carried out spectroscopic, calorimetric microscopic techniques investigate factors that are responsible for structural, morphological alteration protein. Our outcome results show HSA dependent on hydrophobicity, charge temperature, because formation occurs presence a cationic compound, quaternary amine diethylaminoethyl ester (QRMAE), at 40°C pH 7.4 (but 25°C similar value, there no evidence aggregate formation). In addition, parent compound QRMAE, i.e., abietic acid, other derivatives such as nonionic compounds [(RMPEG-750) (RMA-MPEG-750)] do not shows aggregating property. work provides precise necessary information aid understanding effects derivative HSA. also restrains important athletes, health providers, pharmaceutical companies, industries, soft drink-processing companies.
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