Carboxylic Group Functionalized Carbon Quantum Dots inhibit Hen Egg White Lysozyme Amyloidogenesis, leading to the Formation of Spherical Aggregates with Reduced Toxicity and ROS Generation.

IF 16.4 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
M. P. Prabhu, Shreya Chrungoo, N. Sarkar
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Abstract

INTRODUCTION Proteinopathies are a group of diseases where the protein structure has been altered. These alterations are linked to the production of amyloids, which are persistent, organized clumps of protein molecules through inter-molecular interactions. Several disorders, including Alzheimer's and Parkinson's, have been related to the presence of amyloids. Highly ordered beta sheets or beta folds are characteristic of amyloids; these structures can further self- -assemble into stable fibrils. METHOD Protein aggregation is caused by a wide variety of environmental and experimental factors, including mutations, high pH, high temperature, and chemical modification. Despite several efforts, a cure for amyloidosis has yet to be found. Due to its advantageous semi-conducting characteristics, unique optical features, high surface area-to-volume ratio, biocompatibility, etc., carbon quantum dots (CQDs) have lately emerged as key instruments for a wide range of biomedical applications. To this end, we have investigated the effect of CQDs with a carboxyl group on their surface (CQD-CA) on the in vitro amyloidogenesis of hen egg white lysozyme (HEWL). RESULT By generating a stable compound that is resistant to fibrillation, our findings show that CQD-CA can suppress amyloid and disaggregate HEWL. In addition, CQD-CA caused the creation of non-toxic spherical aggregates, which generated much less reactive oxygen species (ROS). CONCLUSION Overall, our results show that more research into amyloidosis treatments, including surface functionalized CQDs, is warranted.
羧基功能化碳量子点可抑制母鸡卵白溶菌酶淀粉样蛋白生成,从而形成球形聚集体,降低毒性和 ROS 生成。
简介蛋白质病是一组蛋白质结构发生改变的疾病。这些改变与淀粉样蛋白的产生有关,淀粉样蛋白是蛋白质分子通过分子间相互作用而形成的持久的、有组织的团块。包括阿尔茨海默氏症和帕金森氏症在内的多种疾病都与淀粉样蛋白的存在有关。高度有序的贝塔片或贝塔折叠是淀粉样蛋白的特征;这些结构可进一步自我组装成稳定的纤维。尽管经过多次努力,但淀粉样变性的治疗方法仍未找到。碳量子点(CQDs)因其优越的半导电特性、独特的光学特征、高表面积体积比、生物相容性等优点,近年来已成为广泛生物医学应用的关键工具。为此,我们研究了表面带有羧基的碳量子点(CQD-CA)对母鸡卵白溶菌酶(HEWL)体外淀粉样蛋白生成的影响。结果表明,通过生成一种抗纤维化的稳定化合物,CQD-CA 可以抑制淀粉样蛋白并分解 HEWL。此外,CQD-CA 还能产生无毒的球形聚集体,其产生的活性氧(ROS)也要少得多。总之,我们的研究结果表明,有必要对淀粉样变性治疗方法(包括表面功能化 CQDs)进行更多研究。
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来源期刊
Accounts of Chemical Research
Accounts of Chemical Research 化学-化学综合
CiteScore
31.40
自引率
1.10%
发文量
312
审稿时长
2 months
期刊介绍: Accounts of Chemical Research presents short, concise and critical articles offering easy-to-read overviews of basic research and applications in all areas of chemistry and biochemistry. These short reviews focus on research from the author’s own laboratory and are designed to teach the reader about a research project. In addition, Accounts of Chemical Research publishes commentaries that give an informed opinion on a current research problem. Special Issues online are devoted to a single topic of unusual activity and significance. Accounts of Chemical Research replaces the traditional article abstract with an article "Conspectus." These entries synopsize the research affording the reader a closer look at the content and significance of an article. Through this provision of a more detailed description of the article contents, the Conspectus enhances the article's discoverability by search engines and the exposure for the research.
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