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Peptide–protein interactions studied by surface plasmon and nuclear magnetic resonances
Author(s) -
Spiga Ottavia,
Bernini Andrea,
Scarselli Maria,
Ciutti Arianna,
Bracci Luisa,
Lozzi Luisa,
Lelli Barbara,
Di Maro Daniela,
Calamandrei Duccio,
Niccolai Neri
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03274-4
Subject(s) - surface plasmon resonance , chemistry , intramolecular force , affinities , peptide , nuclear overhauser effect , nicotinic acetylcholine receptor , nuclear magnetic resonance spectroscopy , acetylcholine receptor , protein structure , dissociation (chemistry) , nuclear magnetic resonance , stereochemistry , receptor , nanotechnology , biochemistry , materials science , physics , nanoparticle
The structural features of the complexes that α‐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.