胺基表面功能化碳量子点通过诱导无毒球形聚集体的形成对母鸡蛋清溶菌酶表现出抗淀粉样蛋白生成作用。

IF 1.9 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
M. P. Taraka Prabhu, Shreya Chrungoo, Nandini Sarkar
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引用次数: 0

摘要

多肽链偏离其传统的蛋白质折叠途径,转而作为非途径中间体被捕获的趋势,一直是一个备受关注的问题。这些非途径中间体最终导致形成称为淀粉样蛋白的不溶性有序原纤维聚集体,淀粉样蛋白导致阿尔茨海默病、帕金森病和II型糖尿病等一系列神经退行性疾病。尽管进行了广泛的研究,但开发一种有效的治疗淀粉样变性的策略仍然难以捉摸。近年来,碳量子点(CQD)因其易于制备、水溶性、独特的光学性质、高表面积比、理化性质、半导电性和主要的生物相容性而引起了研究人员对淀粉样变性的关注。在目前的研究中,我们报道了一种易于制备的方法,用于从常用的具有抗氧化性能的厨房香料中合成胺基表面功能化CQD。评价了所合成的CQD对母鸡蛋清溶菌酶(HEWL)的抗淀粉样变性特性。我们的结果清楚地表明,表面功能化的CQD能够与HEWL相互作用,从而形成稳定的复合物,该复合物对淀粉样蛋白的形成具有抗性,并导致无毒球状聚集体的形成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Amine Group Surface-Functionalized Carbon Quantum Dots Exhibit Anti-amyloidogenic Effects Towards Hen Egg White Lysozyme by Inducing Formation of Nontoxic Spherical Aggregates

Amine Group Surface-Functionalized Carbon Quantum Dots Exhibit Anti-amyloidogenic Effects Towards Hen Egg White Lysozyme by Inducing Formation of Nontoxic Spherical Aggregates

The tendency of polypeptide chains to deviate from their conventional protein folding pathway and instead get trapped as off-pathway intermediates, has been a matter of great concern. These off-pathway intermediates eventually lead to the formation of insoluble, ordered fibrillar aggregates called amyloids, which are responsible for a host of neurodegenerative diseases like Alzheimer’s disease, Parkinson’s disease and Type II diabetes. In spite of extensive research, development of an effective therapeutic strategy against amyloidosis still remains elusive. In recent times, carbon quantum dots (CQD) have grabbed the attention of researchers against amyloidogenesis due to their ease of preparation, aqueous soluble nature, unique optical properties, high surface to volume ratio, physio-chemical properties, semi-conducting nature and mainly biocompatible. In the current study, we have reported an easy-to-prepare procedure for synthesis of amine group surface functionalized CQDs from commonly available kitchen spices with anti-oxidant properties. The as-synthesized CQDs were evaluated for their anti-amyloidogenic properties towards Hen Egg White Lysozyme (HEWL). Our results clearly show that the surfaced functionalized CQDs were able to interact with HEWL, thereby forming a stable complex, which was resistant towards amyloid formation and instead lead to the formation of non-toxic globular aggregates.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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