The Pathway of Amyloid Aggregation of Titin

IF 4.033 Q4 Biochemistry, Genetics and Molecular Biology Biophysics Pub Date : 2024-03-18 DOI:10.1134/S0006350923060039
L. G. Bobyleva, T. A. Uryupina, M. A. Timchenko, S. N. Udaltsov, I. M. Vikhlyantsev, A. G. Bobylev
{"title":"The Pathway of Amyloid Aggregation of Titin","authors":"L. G. Bobyleva,&nbsp;T. A. Uryupina,&nbsp;M. A. Timchenko,&nbsp;S. N. Udaltsov,&nbsp;I. M. Vikhlyantsev,&nbsp;A. G. Bobylev","doi":"10.1134/S0006350923060039","DOIUrl":null,"url":null,"abstract":"<p>The process of amyloid aggregation is quite complex and poorly studied. In this paper, summarizing the previously obtained results on the aggregation of the multidomain smooth muscle protein titin, we tried to complement the idea of its amyloid aggregation by presenting a new, in our opinion, possible mechanism. The main conclusion is that the ability of titin to form amorphous aggregates seems to be the only possible means of aggregation of this protein. Apparently, only individual sections of the molecules, and not the entire protein, are involved in the formation of the amyloid structure in amorphous aggregates of smooth muscle titin. This feature distinguishes titin from other amyloid or amyloid-like proteins due to the large size of the molecule. The possible energy landscape underlying the formation of amyloid aggregates of titin is discussed.</p>","PeriodicalId":493,"journal":{"name":"Biophysics","volume":null,"pages":null},"PeriodicalIF":4.0330,"publicationDate":"2024-03-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysics","FirstCategoryId":"4","ListUrlMain":"https://link.springer.com/article/10.1134/S0006350923060039","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"Biochemistry, Genetics and Molecular Biology","Score":null,"Total":0}
引用次数: 0

Abstract

The process of amyloid aggregation is quite complex and poorly studied. In this paper, summarizing the previously obtained results on the aggregation of the multidomain smooth muscle protein titin, we tried to complement the idea of its amyloid aggregation by presenting a new, in our opinion, possible mechanism. The main conclusion is that the ability of titin to form amorphous aggregates seems to be the only possible means of aggregation of this protein. Apparently, only individual sections of the molecules, and not the entire protein, are involved in the formation of the amyloid structure in amorphous aggregates of smooth muscle titin. This feature distinguishes titin from other amyloid or amyloid-like proteins due to the large size of the molecule. The possible energy landscape underlying the formation of amyloid aggregates of titin is discussed.

Abstract Image

Abstract Image

查看原文
分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
Titin 的淀粉样蛋白聚集途径
摘要淀粉样蛋白的聚集过程相当复杂,研究也不深入。在本文中,我们总结了以前获得的有关多域平滑肌蛋白 titin 聚集的结果,试图通过提出一种新的、我们认为可能的机制来补充其淀粉样聚集的观点。主要结论是,滴定蛋白形成无定形聚集体的能力似乎是这种蛋白质聚集的唯一可能途径。显然,在平滑肌 titin 的无定形聚集体中,只有分子的个别部分而不是整个蛋白质参与了淀粉样结构的形成。由于分子体积较大,这一特征将 titin 与其他淀粉样或类淀粉样蛋白区分开来。本文讨论了形成泰汀淀粉样聚集体的可能能量图谱。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 去求助
来源期刊
Biophysics
Biophysics Biochemistry, Genetics and Molecular Biology-Biophysics
CiteScore
1.20
自引率
0.00%
发文量
67
期刊介绍: Biophysics is a multidisciplinary international peer reviewed journal that covers a wide scope of problems related to the main physical mechanisms of processes taking place at different organization levels in biosystems. It includes structure and dynamics of macromolecules, cells and tissues; the influence of environment; energy transformation and transfer; thermodynamics; biological motility; population dynamics and cell differentiation modeling; biomechanics and tissue rheology; nonlinear phenomena, mathematical and cybernetics modeling of complex systems; and computational biology. The journal publishes short communications devoted and review articles.
期刊最新文献
Reductive Nitrosylation of Hemoglobin and Myoglobin and its Antioxidant Effect Supercomputer Simulation of Intramolecular Oscillations of Glycine, Diphenylalanine, and Tryptophan in an Electric Field of the Terahertz and Infrared Ranges On the Role of Priming in the Development of Modern Rehabilitation Technologies The Inhibitory Effect of Oxibiol on the Process of Protein Modification by Water-Soluble Products of Photo-Oxidative Destruction of Bisretinoid A2E An X-Ray Diffraction Study of Lipid Films with ICHPHAN
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
现在去查看 取消
×
提示
确定
0
微信
客服QQ
Book学术公众号 扫码关注我们
反馈
×
意见反馈
请填写您的意见或建议
请填写您的手机或邮箱
已复制链接
已复制链接
快去分享给好友吧!
我知道了
×
扫码分享
扫码分享
Book学术官方微信
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术
文献互助 智能选刊 最新文献 互助须知 联系我们:info@booksci.cn
Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。
Copyright © 2023 Book学术 All rights reserved.
ghs 京公网安备 11010802042870号 京ICP备2023020795号-1