【摘 要】
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This study presents an analysis of the thermal aggregation of human serum albumin (HSA) induced by novel rosin compounds.The aggregation process causes conformational alterations in the secondary and
【机 构】
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Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh, India
【出 处】
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The 9th Asian Biophysics Association Symposium (ABA2015)(第九届
论文部分内容阅读
This study presents an analysis of the thermal aggregation of human serum albumin (HSA) induced by novel rosin compounds.The aggregation process causes conformational alterations in the secondary and tertiary structures of proteins.In this study, the conversion of globular protein to amorphous aggregates was followed by spectroscopic and microscopic techniques to investigate factors that are responsible for the structural and conformational change and morphology of the proteins.Our results show that the aggregation of HSA was dependent on hydrophobicity, charge and temperature because the formation of amorphous aggregates occurs in the presence of a novel cationic rosin compound, quatemary amine of rosin diethylaminoethyl ester (QRMAE), at 40 oC and pH 7.4 (at 25 oC, there was no evidence of aggregate formation).In addition, the parent compound of QRMAE, abietic acid, and other nonionic rosin compounds [ester of rosin acid with polyethylene glycol monomethyl ether (RMPEG-750) and ester of rosin maleic anhydride with polyethylene glycol monomethyl ether (RMA-MPEG-750)]do not show this property.This work provides precise and necessary information to aid in the understanding the effects of rosin compounds on HSA.This study also provides important information for athletes, health providers, pharmaceutical companies, industries, and soft drink-processing companies.
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