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碳量子点通过形成稳定的蛋白质复合物对蛋清溶菌酶淀粉样变的抑制作用。

Inhibitory effects of carbon quantum dots towards hen egg white lysozyme amyloidogenesis through formation of a stable protein complex.

作者信息

Prabhu M P Taraka, Sarkar Nandini

机构信息

Department of Biotechnology and Medical Engineering, National Institute of Technology Rourkela, Rourkela 769008, Odisha, India.

Department of Biotechnology and Medical Engineering, National Institute of Technology Rourkela, Rourkela 769008, Odisha, India.

出版信息

Biophys Chem. 2022 Jan;280:106714. doi: 10.1016/j.bpc.2021.106714. Epub 2021 Nov 1.

DOI:10.1016/j.bpc.2021.106714
PMID:34749221
Abstract

Proteins, under certain circumstances such as defective quality control mechanism, mutations and altered environmental conditions, undergo misfolding and assemble into highly ordered beta-sheet structured fibrillar aggregates called amyloid fibrils. Formation of amyloid is seen in most of the protein linked degenerative diseases like Alzheimer's disease, Parkinson's disease, Huntington's disease, Type II diabetes mellitus and many more. Amyloid fibril forms via intermediate state(s), and is known to follow a nucleated condensation polymerization mechanism. Though extensive research is being carried out towards finding a therapeutic solution to the amyloidosis, an effective treatment to these diseases still remains elusive and also the mechanism of amyloidogenesis largely remains unclear. In recent times, carbon quantum dots (CQDs) are gaining the attention of researchers due to their semi-conductive nature, excellent physio-chemical properties, high surface to volume ratio, optical properties and mainly bio-compatibility. In the current study, we have synthesized CQDs from commonly available kitchen spice mix and explored their role in amyloidogenesis using hen egg white lysozyme (HEWL) as a model protein. The results clearly demonstrate the amyloid inhibitory as well as disaggregation potential of CQD by forming a stable complex with HEWL and thereby increasing the energy barrier for the aggregation process.

摘要

在某些情况下,如质量控制机制缺陷、突变和环境条件改变,蛋白质会发生错误折叠,并组装成高度有序的β-折叠结构的纤维状聚集体,称为淀粉样纤维。在大多数与蛋白质相关的退行性疾病中都能看到淀粉样蛋白的形成,如阿尔茨海默病、帕金森病、亨廷顿舞蹈症、II型糖尿病等等。淀粉样纤维通过中间状态形成,已知遵循成核凝聚聚合机制。尽管人们正在广泛开展研究以寻找治疗淀粉样变性的方法,但这些疾病的有效治疗方法仍然难以捉摸,而且淀粉样蛋白生成的机制在很大程度上仍不清楚。近年来,碳量子点(CQDs)因其半导体性质、优异的物理化学性质、高比表面积、光学性质以及主要的生物相容性而受到研究人员的关注。在本研究中,我们从常见的厨房香料混合物中合成了碳量子点,并以蛋清溶菌酶(HEWL)作为模型蛋白,探讨了它们在淀粉样蛋白生成中的作用。结果清楚地表明,碳量子点通过与HEWL形成稳定的复合物,从而增加聚集过程的能量屏障,具有抑制淀粉样蛋白生成以及解聚的潜力。

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