钙离子不会影响 Aβ(25-35)引发的脂膜形态变化。

IF 3.3 3区 生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY
Sergei Kurakin , Oleksandr Ivankov , Ermuhammad Dushanov , Tatiana Murugova , Elena Ermakova , Sergey Efimov , Timur Mukhametzyanov , Svetlana Smerdova , Vladimir Klochkov , Alexander Kuklin , Norbert Kučerka
{"title":"钙离子不会影响 Aβ(25-35)引发的脂膜形态变化。","authors":"Sergei Kurakin ,&nbsp;Oleksandr Ivankov ,&nbsp;Ermuhammad Dushanov ,&nbsp;Tatiana Murugova ,&nbsp;Elena Ermakova ,&nbsp;Sergey Efimov ,&nbsp;Timur Mukhametzyanov ,&nbsp;Svetlana Smerdova ,&nbsp;Vladimir Klochkov ,&nbsp;Alexander Kuklin ,&nbsp;Norbert Kučerka","doi":"10.1016/j.bpc.2024.107292","DOIUrl":null,"url":null,"abstract":"<div><p>We have studied the effect of calcium ions (Ca<sup>2+</sup>) at various concentrations on the structure of lipid vesicles in the presence of amyloid-beta peptide Aβ(25–35). In particular, we have investigated the influence of calcium ions on the formation of recently documented bicelle-like structures (BLSs) emerged as a result of Aβ(25–35) triggered membrane disintegration. First, we have shown by using small-angle X-ray and neutron scattering that peptide molecules rigidify the lipid bilayer of gel phase DPPC unilamellar vesicles (ULVs), while addition of the calcium ions to the system hinders this effect of Aβ(25–35). Secondly, the Aβ(25–35) demonstrates a critical peptide concentration at which the BLSs reorganize from ULVs due to heating and cooling the samples through the lipid main phase transition temperature (<em>T</em><sub><em>m</em></sub>). However, addition of calcium ions does not affect noticeably the Aβ-induced formation of BLSs and their structural parameters, though the changes in peptide's secondary structure, e.g. the increased α-helix fraction, has been registered by circular dichroism spectroscopy. Finally, according to <sup>31</sup>P nuclear magnetic resonance (NMR) measurements, calcium ions do not affect the lipid-peptide arrangement in BLSs and their ability to align in the magnetic field of NMR spectrometer. The influences of various concentrations of calcium ions on the lipid-peptide interactions may prove biologically important because their local concentrations vary widely in <em>in-vivo</em> conditions. In the present work, calcium ions were investigated as a possible tool aimed at regulating the lipid-peptide interactions that demonstrated the disruptive effect of Aβ(25–35) on lipid membranes.</p></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"313 ","pages":"Article 107292"},"PeriodicalIF":3.3000,"publicationDate":"2024-07-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Calcium ions do not influence the Aβ(25–35) triggered morphological changes of lipid membranes\",\"authors\":\"Sergei Kurakin ,&nbsp;Oleksandr Ivankov ,&nbsp;Ermuhammad Dushanov ,&nbsp;Tatiana Murugova ,&nbsp;Elena Ermakova ,&nbsp;Sergey Efimov ,&nbsp;Timur Mukhametzyanov ,&nbsp;Svetlana Smerdova ,&nbsp;Vladimir Klochkov ,&nbsp;Alexander Kuklin ,&nbsp;Norbert Kučerka\",\"doi\":\"10.1016/j.bpc.2024.107292\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>We have studied the effect of calcium ions (Ca<sup>2+</sup>) at various concentrations on the structure of lipid vesicles in the presence of amyloid-beta peptide Aβ(25–35). In particular, we have investigated the influence of calcium ions on the formation of recently documented bicelle-like structures (BLSs) emerged as a result of Aβ(25–35) triggered membrane disintegration. First, we have shown by using small-angle X-ray and neutron scattering that peptide molecules rigidify the lipid bilayer of gel phase DPPC unilamellar vesicles (ULVs), while addition of the calcium ions to the system hinders this effect of Aβ(25–35). Secondly, the Aβ(25–35) demonstrates a critical peptide concentration at which the BLSs reorganize from ULVs due to heating and cooling the samples through the lipid main phase transition temperature (<em>T</em><sub><em>m</em></sub>). However, addition of calcium ions does not affect noticeably the Aβ-induced formation of BLSs and their structural parameters, though the changes in peptide's secondary structure, e.g. the increased α-helix fraction, has been registered by circular dichroism spectroscopy. Finally, according to <sup>31</sup>P nuclear magnetic resonance (NMR) measurements, calcium ions do not affect the lipid-peptide arrangement in BLSs and their ability to align in the magnetic field of NMR spectrometer. The influences of various concentrations of calcium ions on the lipid-peptide interactions may prove biologically important because their local concentrations vary widely in <em>in-vivo</em> conditions. In the present work, calcium ions were investigated as a possible tool aimed at regulating the lipid-peptide interactions that demonstrated the disruptive effect of Aβ(25–35) on lipid membranes.</p></div>\",\"PeriodicalId\":8979,\"journal\":{\"name\":\"Biophysical chemistry\",\"volume\":\"313 \",\"pages\":\"Article 107292\"},\"PeriodicalIF\":3.3000,\"publicationDate\":\"2024-07-11\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biophysical chemistry\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0301462224001212\",\"RegionNum\":3,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biophysical chemistry","FirstCategoryId":"99","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0301462224001212","RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

我们研究了不同浓度的钙离子(Ca2+)对存在淀粉样β肽Aβ(25-35)的脂质囊泡结构的影响。特别是,我们研究了钙离子对最近记录的因淀粉样β肽Aβ(25-35)引发的膜解体而形成的双核样结构(BLSs)的影响。首先,我们利用小角 X 射线和中子散射证明,肽分子能使凝胶相 DPPC 单拉美米尔囊泡的脂质双分子层僵化,而钙离子的加入则会阻碍 Aβ(25-35)的这种作用。其次,Aβ(25-35)显示了一个临界肽浓度,在该浓度下,由于加热和冷却样品使其达到脂质主相转变温度(Tm),BLS 从 ULV 重组。然而,加入钙离子并不会明显影响 Aβ 诱导的 BLS 的形成及其结构参数,尽管圆二色谱法记录了肽二级结构的变化,如 α 螺旋部分的增加。最后,根据 31P 核磁共振(NMR)测量,钙离子不会影响 BLS 中脂肽的排列及其在 NMR 光谱仪磁场中的排列能力。不同浓度的钙离子对脂肽相互作用的影响可能具有重要的生物学意义,因为钙离子在体内的局部浓度变化很大。本研究将钙离子作为调节脂质-肽相互作用的一种可能工具进行研究,结果表明 Aβ(25-35)对脂质膜具有破坏作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Calcium ions do not influence the Aβ(25–35) triggered morphological changes of lipid membranes

Calcium ions do not influence the Aβ(25–35) triggered morphological changes of lipid membranes

We have studied the effect of calcium ions (Ca2+) at various concentrations on the structure of lipid vesicles in the presence of amyloid-beta peptide Aβ(25–35). In particular, we have investigated the influence of calcium ions on the formation of recently documented bicelle-like structures (BLSs) emerged as a result of Aβ(25–35) triggered membrane disintegration. First, we have shown by using small-angle X-ray and neutron scattering that peptide molecules rigidify the lipid bilayer of gel phase DPPC unilamellar vesicles (ULVs), while addition of the calcium ions to the system hinders this effect of Aβ(25–35). Secondly, the Aβ(25–35) demonstrates a critical peptide concentration at which the BLSs reorganize from ULVs due to heating and cooling the samples through the lipid main phase transition temperature (Tm). However, addition of calcium ions does not affect noticeably the Aβ-induced formation of BLSs and their structural parameters, though the changes in peptide's secondary structure, e.g. the increased α-helix fraction, has been registered by circular dichroism spectroscopy. Finally, according to 31P nuclear magnetic resonance (NMR) measurements, calcium ions do not affect the lipid-peptide arrangement in BLSs and their ability to align in the magnetic field of NMR spectrometer. The influences of various concentrations of calcium ions on the lipid-peptide interactions may prove biologically important because their local concentrations vary widely in in-vivo conditions. In the present work, calcium ions were investigated as a possible tool aimed at regulating the lipid-peptide interactions that demonstrated the disruptive effect of Aβ(25–35) on lipid membranes.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Biophysical chemistry
Biophysical chemistry 生物-生化与分子生物学
CiteScore
6.10
自引率
10.50%
发文量
121
审稿时长
20 days
期刊介绍: Biophysical Chemistry publishes original work and reviews in the areas of chemistry and physics directly impacting biological phenomena. Quantitative analysis of the properties of biological macromolecules, biologically active molecules, macromolecular assemblies and cell components in terms of kinetics, thermodynamics, spatio-temporal organization, NMR and X-ray structural biology, as well as single-molecule detection represent a major focus of the journal. Theoretical and computational treatments of biomacromolecular systems, macromolecular interactions, regulatory control and systems biology are also of interest to the journal.
×
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
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
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 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信