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离子强度对鸡卵清溶菌酶淀粉样纤维形成的影响。

Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme.

机构信息

Department of Physical Chemistry, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, Gdańsk 80-233, Poland.

Department of Electrochemistry, Corrosion and Materials Engineering, Faculty of Chemistry, Gdańsk University of Technology, Narutowicza Str. 11/12, Gdańsk 80-233, Poland.

出版信息

Int J Biol Macromol. 2019 Jan;121:63-70. doi: 10.1016/j.ijbiomac.2018.09.165. Epub 2018 Oct 2.

DOI:10.1016/j.ijbiomac.2018.09.165
PMID:30290259
Abstract

The study investigates the role of the electrostatic interactions in the fibrillation of the hen egg white lysozyme (HEWL). In order to achieve this aim the influence of the cations Na, Mg and Al on the amyloid fibril formation and amorphous aggregation was tested. The amyloids are formed in the solution without added salt but the Thioflavin T fluorescence gives the false-negative result. In these conditions, the HEWL fibrils are long and curvy. If the ionic strength of the solution is sufficiently high, the formed amyloids are shorter and fragmented. Our study shows that the addition of the aluminium salt promotes protein fibrillation. The amorphous aggregation dominates in the high concentration of electrolyte. The in vitro amyloid fibril formation seems to be regulated by universal mechanisms. The theories implemented in the polymer science or for colloidal solutions give the qualitative description of the aggregation phenomena. However, the specific interactions and the additional effects (e.g. fibril fragmentation) modulate the amyloidogenesis.

摘要

本研究探讨了静电相互作用在鸡卵清溶菌酶(HEWL)纤维化中的作用。为了达到这一目的,测试了阳离子 Na、Mg 和 Al 对淀粉样纤维形成和无定形聚集的影响。淀粉样蛋白是在没有添加盐的溶液中形成的,但 Thioflavin T 荧光给出了假阴性结果。在这些条件下,HEWL 纤维又长又弯。如果溶液的离子强度足够高,则形成的淀粉样蛋白较短且呈碎片状。我们的研究表明,铝盐的添加促进了蛋白质的纤维化。无定形聚集在高浓度电解质中占主导地位。体外淀粉样纤维的形成似乎受到普遍机制的调节。聚合物科学或胶体溶液中实施的理论给出了聚集现象的定性描述。然而,特定的相互作用和附加效应(例如纤维碎片)调节淀粉样蛋白的形成。

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