Department of Biochemistry, Faculty of Life Sciences, Aligarh Muslim University, Aligarh, India.
Cell Biochem Biophys. 2011 Nov;61(2):237-50. doi: 10.1007/s12013-011-9200-x.
The ability of a polypeptide to fold into a unique, functional, and three-dimensional structure depends on the intrinsic properties of the amino acid sequence, function of the molecular chaperones, proteins, and enzymes. Every polypeptide has a finite tendency to misfold and this forms the darker side of the protein world. Partially folded and misfolded proteins that escape the cellular quality control mechanism have the high tendency to form inter-molecular hydrogen bonding between the same protein molecules resulting in aggregation. This review summarizes the underlying and universal mechanism of protein folding. It also deals with the factors responsible for protein misfolding and aggregation. This article describes some of the consequences of such behavior particularly in the context of neurodegenerative conformational diseases such as Alzheimer's, Parkinson's, Huntington's, amyotrophic lateral sclerosis and other non-neurodegenerative conformational diseases such as cancer and cystic fibrosis etc. This will encourage a more proactive approach to the early diagnosis of conformational diseases and nutritional counseling for patients.
多肽折叠成独特、功能和三维结构的能力取决于氨基酸序列的固有特性、分子伴侣、蛋白质和酶的功能。每个多肽都有一定的错误折叠倾向，这构成了蛋白质世界的阴暗面。部分折叠和错误折叠的蛋白质，如果逃脱了细胞质量控制机制，就很容易在同种蛋白质分子之间形成分子间氢键，从而导致聚集。本文总结了蛋白质折叠的基本和普遍机制。它还涉及导致蛋白质错误折叠和聚集的因素。本文描述了这种行为的一些后果，特别是在神经退行性构象疾病（如阿尔茨海默病、帕金森病、亨廷顿病、肌萎缩性侧索硬化症）和非神经退行性构象疾病（如癌症和囊性纤维化等）的背景下。这将鼓励采取更积极的方法来早期诊断构象疾病，并为患者提供营养咨询。
