Interpolyelectrolyte complexes of lysozyme with short poly[di(carboxylatophenoxy)phosphazene]. Binding energetics and protein conformational stability

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• 作者：Tatiana V. Burova^a ; Natalia V. Grinberg^a ; Alexander S. Dubovik^b ; Elena A. Olenichenko^c ; Victor N. Orlov^c ; Valerij Y. Grinberg^b ; ^{grinberg@ineos.ac.ru}
• 关键词：Protein-polyphosphazene interaction ; DSC ; ITC
• 刊名：Polymer
• 出版年：2017
• 出版时间：13 January 2017
• 年：2017
• 卷：108
• 期：Complete
• 页码：97-104
• 全文大小：1023 K
• 卷排序：108

文摘

Binding of lysozyme to short PCPP is cooperative in nature. Electrostatic protein-PCPP and van der Waals protein-protein interactions contribute mainly into the binding energetics. The binding leads to destabilization of the native conformation of protein. The destabilization is much more pronounced for non-stoichiometric Lysozyme-PCPP complexes than for the stoichiometric one.