首页 | 本学科首页   官方微博 | 高级检索  
     


NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin
Authors:Bernini Andrea  Ciutti Arianna  Spiga Ottavia  Scarselli Maria  Klein Samuel  Vannetti Stefano  Bracci Luisa  Lozzi Luisa  Lelli Barbara  Falciani Chiara  Neri Paolo  Niccolai Neri
Affiliation:Biomolecular Structure Research Center and Department of Molecular Biology, University of Siena, via Fiorentina 1, I-53100 Siena, Italy. andrea.bernini@unisi.it
Abstract:The interaction between alpha-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several methods and a wealth of functional, kinetic and structural data are available. Hence, this system represents a suitable model to explore in detail the dynamics of a peptide-protein interaction. Here, the solution structure of a new complex of the protein toxin with a tridecapeptide ligand exhibiting high affinity has been determined by NMR. As observed for three other previously reported mimotope-alpha-bungarotoxin complexes, also in this case correlations between biological activity and kinetic data are not fully consistent with a static discussion of structural data. Molecular dynamics simulations of the four mimotope-toxin complexes indicate that a relevant contribution to the complex stability is given by the extent of the residual flexibility that the protein maintains upon peptide binding. This feature, limiting the entropy loss caused by protein folding and binding, ought to be generally considered in a rational design of specific protein ligands.
Keywords:mimotope   α-bungarotoxin   dynamics   peptide-protein interaction   NMR
本文献已被 ScienceDirect PubMed 等数据库收录!
设为首页 | 免责声明 | 关于勤云 | 加入收藏

Copyright©北京勤云科技发展有限公司  京ICP备09084417号