:Self-attachment of proteins leading to the formation of highly insoluble protein oligomers and aggregates has become an important focus of research owing to its diverse implications in pathophysiology and diseases. This has become a more frequent phenomenon in most neurological and neurodegenerative diseases as well as in dementia. In recent years such event of protein aggregation has linked to other disease conditions, disorders or adverse health conditions. Interestingly, aggregation of protein also plays role in development, growth or metabolism. Most often physiological proteins are initially bio-synthesised in native or nascent geometrical forms or conformations but later they undergo specific folding pattern and thereby acquire a stable configuration that is biologically relevant and active. It is highly important that these proteins remain in their biologically active configuration in order to exert their functional properties. Any alteration or change to this structural configuration can be detrimental to their specific functions and may cause pathological consequences leading to the onset of diseases or disorders. Several factors such as the action of chaperones, binding partners, physiological metal ions, pH level, temperature, ionic strength, interfacial exposure (solid-liquid, liquid-liquid, gas-liquid), mutation and post translational modification, chemical changes, interaction with small molecules such as lipids, hormones, etc. and solvent environment have been either identified or proposed as important factors in conferring the ultimate status of protein structure and configuration. Among many misfolding protein conformations, self-assembly or aggregation is the most significant. It leads to the formation of highly oligomeric self-aggregates that precipitate and interfere with many biochemical processes with serious pathological consequences. The most common implication of protein aggregation leading to the formation of deposits / plaques of various morphological types is the onset of neurological and neurodegenerative diseases that include Alzheimer’s, Parkinson’s, Huntington, ALS (Amyotrophic Lateral Sclerosis), CJD (Creutzfeldt Jakob Dementia), Prion diseases, Amyloidosis and other forms of dementia. However increasingly studies revealed that protein aggregation may also be associated with other diseases such as cancer, type 2 diabetes, renal, corneal and cardiovascular diseases. Protein aggregation diseases are now considered as part of “Proteinopathy” which refers to conditions where proteins become structurally abnormal or fail to fold into stable normal configurations. In this review, we reflect on various aspects of protein self-aggregation, potential underlying causes, mechanism, role of secondary structures, pathological consequences and possible intervention strategies as reported in published literatures.

中文翻译：

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健康和疾病中的蛋白质聚集和自组装

：导致高度不溶性蛋白质寡聚体和聚集体形成的蛋白质自附着由于其在病理生理学和疾病中的多种意义而成为研究的重要焦点。这已成为大多数神经和神经退行性疾病以及痴呆症中更常见的现象。近年来，这种蛋白质聚集事件与其他疾病状况、紊乱或不利的健康状况有关。有趣的是，蛋白质的聚集也在发育、生长或新陈代谢中发挥作用。大多数情况下，生理蛋白质最初以天然或新生的几何形式或构象生物合成，但后来它们经历特定的折叠模式，从而获得具有生物学相关性和活性的稳定构型。这些蛋白质保持其生物活性构型以发挥其功能特性非常重要。对这种结构配置的任何改变或改变都可能对其特定功能有害，并可能导致导致疾病或病症发作的病理后果。几个因素，如伴侣的作用、结合伙伴、生理金属离子、pH 水平、温度、离子强度、界面暴露（固-液、液-液、气-液）、突变和翻译后修饰、化学变化、相互作用小分子如脂质、激素等和溶剂环境已被确定或提出作为赋予蛋白质结构和构型最终状态的重要因素。在许多错误折叠的蛋白质构象中，自组装或聚集是最重要的。它导致形成高度低聚的自聚集体，这些聚集体沉淀并干扰许多具有严重病理后果的生化过程。蛋白质聚集导致形成各种形态类型的沉积物/斑块的最常见含义是神经和神经退行性疾病的发作，包括阿尔茨海默病、帕金森病、亨廷顿病、ALS（肌萎缩性侧索硬化症）、CJD（克雅氏痴呆）、朊病毒疾病、淀粉样变性和其他形式的痴呆。然而，越来越多的研究表明，蛋白质聚集也可能与其他疾病有关，例如癌症、2 型糖尿病、肾脏、角膜和心血管疾病。蛋白质聚集疾病现在被认为是“蛋白质病”的一部分，“蛋白质病”是指蛋白质结构异常或无法折叠成稳定的正常构型的情况。在这篇综述中，我们反思了已发表文献中报道的蛋白质自聚集的各个方面、潜在的根本原因、机制、二级结构的作用、病理后果和可能的干预策略。