Molecular Biophysics and Biophysical Chemistry Group, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
Molecular Biophysics and Biophysical Chemistry Group, Interdisciplinary Biotechnology Unit, Aligarh Muslim University, Aligarh 202002, India.
Int J Biol Macromol. 2018 Jun;112:217-229. doi: 10.1016/j.ijbiomac.2018.01.099. Epub 2018 Jan 31.
The newly synthesized unfolded polypeptide attains its functional and unique three-dimensional conformation through the process of protein folding for which several models have been proposed. The protein misfolding diseases include Alzheimer's, Parkinson's and Cataract which are result of formation of amyloid or amorphous aggregates, respectively. The distinction in morphology shows relation with the melting temperature (T). The temperatures near or slightly higher than Tm induces amyloids while much higher or low temperature mediate amorphous aggregation. The aggregation is not always deleterious rather it also performs several important cellular functions essential for survival wide range of organisms called as functional amyloids. Protein gets modulated by several modulators which mediate the aggregation, acceleration, delay, transformations, inhibition and disaggregation of protein aggregates. The exclusive properties of inhibition and disaggregation displayed by various molecules can be employed to treat the life threatening disorders.
新合成的未折叠多肽通过蛋白质折叠过程获得其功能和独特的三维构象,为此提出了几种模型。蛋白质错误折叠疾病包括阿尔茨海默病、帕金森病和白内障,分别是淀粉样或无定形聚集体形成的结果。形态上的区别与熔点(Tm)有关。接近或略高于 Tm 的温度诱导淀粉样形成,而温度过高或过低则介导无定形聚集。聚集并不总是有害的,它还执行几种对生存至关重要的重要细胞功能,这些功能在称为功能淀粉样蛋白的广泛生物体中都有体现。几种调节剂可以调节蛋白质的聚集、加速、延迟、转化、抑制和去聚集,调节剂可以调节蛋白质的聚集。各种分子所表现出的抑制和去聚集的独特性质,可以用来治疗危及生命的疾病。