Peptide-protein interactions studied by surface plasmon and nuclear magnetic resonances

被引：25
|
作者：
Spiga, O
Bernini, A
Scarselli, M
Ciutti, A
Bracci, L
Lozzi, L
Lelli, B
Di Maro, D
Calamandrei, D
Niccolai, N
机构：
[1] Univ Siena, Biomol Struct Res Ctr, I-53100 Siena, Italy
[2] Univ Siena, Dept Biol Mol, I-53100 Siena, Italy
[3] BIOMODEM Pscrl, I-53100 Siena, Italy
来源：
FEBS LETTERS | 2002年 / 511卷 / 1-3期
关键词：
peptide-protein affinity; protein complex; ligand design; intermolecular nuclear Overhauser effects; nuclear magnetic resonance; surface plasmon resonance;
D O I：
10.1016/S0014-5793(01)03274-4
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The structural features of the complexes that (chi-bungarotoxin forms with three different synthetic peptides, mimotopes of the nicotinic acetylcholine receptor binding site, have been compared to the corresponding nuclear magnetic resonance (NMR) and surface plasmon resonance (SPR) data. For the considered peptides, the observed different affinities towards the toxin could not be accounted simply by static structural considerations. A combined analysis of the SPR- and NMR-derived dynamic parameters shows new correlations between complex formation and dissociation and the overall pattern of intramolecular and intermolecular nuclear Overhauser effects. These features could be crucial for a rational design of protein ligands. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码：33 / 35
页数：3
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