Inhibitors of amyloid fibril formation.

3区 生物学 Q2 Biochemistry, Genetics and Molecular Biology Progress in molecular biology and translational science Pub Date : 2024-01-01 Epub Date: 2024-04-22 DOI:10.1016/bs.pmbts.2024.03.012
Elaheh Tavili, Fatemeh Aziziyan, Khosro Khajeh
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Abstract

Many diseases are caused by misfolded and denatured proteins, leading to neurodegenerative diseases. In recent decades researchers have developed a variety of compounds, including polymeric inhibitors and natural compounds, antibodies, and chaperones, to inhibit protein aggregation, decrease the toxic effects of amyloid fibrils, and facilitate refolding proteins. The causes and mechanisms of amyloid formation are still unclear, and there are no effective treatments for Amyloid diseases. This section describes research and achievements in the field of inhibiting amyloid accumulation and also discusses the importance of various strategies in facilitating the removal of aggregates species (refolding) in the treatment of neurological diseases such as chemical methods like as, small molecules, metal chelators, polymeric inhibitors, and nanomaterials, as well as the use of biomolecules (peptide and, protein, nucleic acid, and saccharide) as amyloid inhibitors, are also highlighted.

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淀粉样蛋白纤维形成抑制剂。
许多疾病都是由错误折叠和变性的蛋白质引起的,从而导致神经退行性疾病。近几十年来,研究人员开发了多种化合物,包括高分子抑制剂和天然化合物、抗体和伴侣素,以抑制蛋白质的聚集,降低淀粉样纤维的毒性作用,并促进蛋白质的重新折叠。淀粉样蛋白形成的原因和机制尚不清楚,淀粉样蛋白疾病也没有有效的治疗方法。本节介绍了在抑制淀粉样蛋白积累领域的研究和成就,还讨论了在治疗神经系统疾病中促进清除聚集物种(重折叠)的各种策略的重要性,如化学方法,如小分子、金属螯合剂、聚合物抑制剂和纳米材料,以及使用生物大分子(肽和蛋白质、核酸和糖类)作为淀粉样蛋白抑制剂。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
CiteScore
6.90
自引率
0.00%
发文量
0
审稿时长
>12 weeks
期刊介绍: Progress in Molecular Biology and Translational Science (PMBTS) provides in-depth reviews on topics of exceptional scientific importance. If today you read an Article or Letter in Nature or a Research Article or Report in Science reporting findings of exceptional importance, you likely will find comprehensive coverage of that research area in a future PMBTS volume.
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