A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide.

G Siligardi, A F Drake, P Mascagni, D J Rowlands, F Brown, W A Gibbons
{"title":"A CD strategy for the study of polypeptide folding/unfolding. A synthetic foot-and-mouth disease virus immunogenic peptide.","authors":"G Siligardi,&nbsp;A F Drake,&nbsp;P Mascagni,&nbsp;D J Rowlands,&nbsp;F Brown,&nbsp;W A Gibbons","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>The circular dichroism spectrum of the 20-residue immunogenic peptide from the foot-and-mouth disease virus (VP1; 141-160 of serotype A, subtype 12) was solvent- and temperature-dependent. Careful solvent titration revealed two isodichroic points and plateaux consistent with stepwise unfolding of specific stable conformations. Variable temperature studies in cryogenic solvents and urea perturbation were consistent with the existence of three conformational moieties, the left-handed extended helix, the alpha-helix, and the 3(10) helix. The number of residues in each helix was confirmed by CD spectral simulations. The strategy described here can be used to determine the components of a conformational equilibrium and their statistical weights, to study peptide folding and unfolding and to determine the bioactive conformation(s) of linear peptides. The conclusions were supported by 2D-NMR studies. A new mechanism for the stabilization of left-handed extended helices and destabilization of alpha-helices by urea is proposed. The structure of the peptide as resolved by CD spectroscopy is of particular significance since the conformation of this antigenic sequence in situ has so far not been solved by X-ray crystallography.</p>","PeriodicalId":14204,"journal":{"name":"International journal of peptide and protein research","volume":"38 6","pages":"519-27"},"PeriodicalIF":0.0000,"publicationDate":"1991-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"International journal of peptide and protein research","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0

Abstract

The circular dichroism spectrum of the 20-residue immunogenic peptide from the foot-and-mouth disease virus (VP1; 141-160 of serotype A, subtype 12) was solvent- and temperature-dependent. Careful solvent titration revealed two isodichroic points and plateaux consistent with stepwise unfolding of specific stable conformations. Variable temperature studies in cryogenic solvents and urea perturbation were consistent with the existence of three conformational moieties, the left-handed extended helix, the alpha-helix, and the 3(10) helix. The number of residues in each helix was confirmed by CD spectral simulations. The strategy described here can be used to determine the components of a conformational equilibrium and their statistical weights, to study peptide folding and unfolding and to determine the bioactive conformation(s) of linear peptides. The conclusions were supported by 2D-NMR studies. A new mechanism for the stabilization of left-handed extended helices and destabilization of alpha-helices by urea is proposed. The structure of the peptide as resolved by CD spectroscopy is of particular significance since the conformation of this antigenic sequence in situ has so far not been solved by X-ray crystallography.

分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
用于多肽折叠/展开研究的CD策略。一种合成的口蹄疫病毒免疫原肽。
口蹄疫病毒(VP1) 20残基免疫原肽的圆二色谱分析血清型A的141-160,亚型12)依赖于溶剂和温度。仔细的溶剂滴定发现了两个等向色点和平台,与特定稳定构象的逐步展开一致。在低温溶剂和尿素扰动下的变温研究证实了三种构象的存在,即左旋扩展螺旋、α -螺旋和3(10)螺旋。通过CD谱模拟确定了每个螺旋中的残基数。这里描述的策略可用于确定构象平衡的组成部分及其统计权重,研究肽折叠和展开,并确定线性肽的生物活性构象。这些结论得到了二维核磁共振研究的支持。提出了左旋扩展螺旋稳定和α -螺旋被尿素破坏的新机制。由于该抗原序列的原位构象迄今尚未由x射线晶体学解决,因此用CD光谱解析的肽的结构具有特别重要的意义。
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
自引率
0.00%
发文量
0
期刊最新文献
Noninvasive continuous monitoring of solid-phase peptide synthesis by acid-base indicator. Effect of aromatic amino acid substitutions in the 3-position of cyclic beta-casomorphin analogues on mu-opioid agonist/delta-opioid antagonist properties. Conformational investigation of alpha,beta-dehydropeptides. VII. Conformation of Ac-Pro-deltaAla-NHCH3 and Ac-Pro-(E)-deltaAbu-NHCH3: comparison with (Z)-substituted alpha,beta-dehydropeptides. Protease-catalyzed synthesis of Leu-enkephalin in a solvent-free system. beta-endorphin1-31 in the rat pituitary.
×
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