Amyloid oligomers and their membrane toxicity - A perspective study

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC
Alessandro Nutini
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引用次数: 0

Abstract

Amyloidosis is a condition involving a disparate group of pathologies characterized by the extracellular deposition of insoluble fibrils composed of broken-down proteins. These proteins can accumulate locally, causing peculiar symptoms, or in a widespread way, involving many organs and.

causing severe systemic failure. The damage that is created is related not only to the accumulation of.

amyloid fibrils but above all to the precursor oligomers of the fibrils that manage to enter the cell in a very particular way. This article analyzes the current state of research related to the entry of these oligomers into the cell membrane and the theories related to their toxicity. The paper proposed here not only aims to review the contents in the literature but also proposes a new vision of amyloid toxicity.

that could occur in a multiphase process catalyzed by the cell membrane itself. In this process, the denaturation of the lipid bilayer is followed by the stabilization of a pore through energetically favorable self-assembly processes which are achieved through particular oligomeric structures.

淀粉样蛋白寡聚体及其膜毒性--一项透视研究
淀粉样变性是一种涉及不同病理类型的疾病,其特征是由分解蛋白质组成的不溶性纤维在细胞外沉积。这些蛋白质可以在局部积聚,引起特殊症状,也可以大范围积聚,累及多个器官,造成严重的全身衰竭。所造成的损害不仅与淀粉样蛋白纤维的堆积有关,而且首先与以非常特殊的方式进入细胞的纤维前体低聚物有关。本文分析了与这些低聚物进入细胞膜有关的研究现状,以及与它们的毒性有关的理论。本文不仅回顾了文献内容,还提出了淀粉样蛋白毒性的新观点,即淀粉样蛋白毒性可能发生在细胞膜本身催化的多相过程中。在这一过程中,脂质双分子层变性后,通过能量上有利的自组装过程稳定了一个孔道,该孔道是通过特殊的低聚物结构实现的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
CiteScore
7.20
自引率
4.30%
发文量
567
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