Conformational analysis of peptide surrogates. Reduced and retro-amide links in blocked alanine and in secondary structures.

P Dauber-Osguthorpe, M M Campbell, D J Osguthorpe
{"title":"Conformational analysis of peptide surrogates. Reduced and retro-amide links in blocked alanine and in secondary structures.","authors":"P Dauber-Osguthorpe,&nbsp;M M Campbell,&nbsp;D J Osguthorpe","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>We have investigated the conformational effects of modifying the amide link of peptides. We studied a reverse amide bond psi [NHCO], a reduced amide bond psi [CH2NH] and a retro-reduced bond psi [NHCH2] as surrogates for the amide link [CONH] in native peptides. A complete search of the conformational space available to residues with these modified links was carried out. The local minima and the rotational barriers were described and compared to the minima of the native residue. The results are compatible with the available observed structural data. These modified links have been incorporated in secondary structure units such as beta turns, alpha helices, and parallel and anti-parallel beta sheets. It was found that a reduced amide link can lead to stabilised beta turns, while the retro modification can be incorporated in stable beta sheets. A significant reduction in the stability of alpha helices is caused by the retro links, while a reduced amide link results in only a small destabilisation.</p>","PeriodicalId":14204,"journal":{"name":"International journal of peptide and protein research","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1991-10-01","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

We have investigated the conformational effects of modifying the amide link of peptides. We studied a reverse amide bond psi [NHCO], a reduced amide bond psi [CH2NH] and a retro-reduced bond psi [NHCH2] as surrogates for the amide link [CONH] in native peptides. A complete search of the conformational space available to residues with these modified links was carried out. The local minima and the rotational barriers were described and compared to the minima of the native residue. The results are compatible with the available observed structural data. These modified links have been incorporated in secondary structure units such as beta turns, alpha helices, and parallel and anti-parallel beta sheets. It was found that a reduced amide link can lead to stabilised beta turns, while the retro modification can be incorporated in stable beta sheets. A significant reduction in the stability of alpha helices is caused by the retro links, while a reduced amide link results in only a small destabilisation.

分享 分享
微信好友 朋友圈 QQ好友 复制链接
本刊更多论文
肽替代物的构象分析。阻断丙氨酸和二级结构中的减少和反酰胺连接。
我们研究了修饰肽的酰胺键对构象的影响。我们研究了一个反酰胺键psi [NHCO],一个还原酰胺键psi [CH2NH]和一个还原酰胺键psi [NHCH2]作为天然肽中酰胺键[CONH]的替代品。对具有这些修饰链的残基的构象空间进行了完整的搜索。描述了局部极小值和旋转势垒,并与自然残差的极小值进行了比较。计算结果与现有的结构观测数据一致。这些改进的连杆已被纳入二级结构单元,如β匝、α螺旋、平行和反平行β片。研究发现,减少酰胺连接可以导致稳定的β转,而复古修饰可以纳入稳定的β片。α螺旋稳定性的显著降低是由复古连接引起的,而酰胺连接的减少只会导致小的不稳定性。
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