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Facile preparation of tertiary amine grafted poly (α,β-L-aspartic acid) with zwitterionic property to limit nonspecific protein adsorption
Journal of Dispersion Science and Technology ( IF 2.2 ) Pub Date : 2020-08-14 , DOI: 10.1080/01932691.2020.1805331
Xiaojuan Wang 1 , Hanqing Gu 1 , Guolin Wu 2
Affiliation  

Abstract

A series of poly (amino acid) with zwitterionic character was prepared for surface coating to avoid protein adsorption, by modifying the poly (aspartic acid) side chain with tertiary amine groups. An interesting and facile procedure is described with starts with polysuccinic acid which is followed by ring-opening with amino functions and finally hydrolysis of the remaining succinic acid groups achieving the polyaspartic acid structure as backbone. The degree of cationic tertiary amino group was easily varied by the degree of ring-opening with amines. The materials show isoelectric point between pH 4 and 9, have a typical zwitterionic character, and can be used to coat negatively as well as positively charged surfaces, depending on composition. The protein adsorption behavior is thus pH dependent and was studied with various proteins mainly available in blood. The adsorption test proved that a significant reduction of protein adsorption could be found for fibrinogen and albumin, and this protein-repellent behavior is strongly dependent on the amount of the absorbed polymer (adsorbed at pH = 7.4). This is a nice additional contribution to polymers with zwitterionic character used as coating reducing nonspecific protein adsorption.



中文翻译:

具有两性离子特性以限制非特异性蛋白质吸附的叔胺接枝聚(α,β-L-天冬氨酸)的简便制备

摘要

通过用叔胺基团修饰聚(天冬氨酸)侧链,制备了一系列具有两性离子特性的聚(氨基酸)用于表面涂层以避免蛋白质吸附。描述了一种有趣且简便的程序,从聚琥珀酸开始,然后用氨基官能团开环,最后水解剩余的琥珀酸基团,实现聚天冬氨酸结构作为主链。阳离子叔氨基的程度很容易随胺的开环程度而变化。这些材料的等电点在 pH 4 和 9 之间,具有典型的两性离子特性,可用于涂覆带负电和带正电的表面,具体取决于成分。因此,蛋白质吸附行为依赖于 pH 值,并用主要存在于血液中的各种蛋白质进行了研究。吸附试验证明,纤维蛋白原和白蛋白的蛋白质吸附显着减少,这种蛋白质排斥行为强烈依赖于吸收的聚合物的量(在 pH = 7.4 时吸附)。这是对用作涂层的具有两性离子特性的聚合物减少非特异性蛋白质吸附的一个很好的额外贡献。

更新日期:2020-08-14
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