Peptide-protein interactions studied by surface plasmon and nuclear magnetic resonances.
The structural features of the complexes that alpha-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.
Spiga
Ottavia
O
Biomolecular Structure Research Center and Department of Molecular Biology, University of Siena, Siena, Italy.
Bernini
Andrea
A
Scarselli
Maria
M
Ciutti
Arianna
A
Bracci
Luisa
L
Lozzi
Luisa
L
Lelli
Barbara
B
Di Maro
Daniela
D
Calamandrei
Duccio
D
Niccolai
Neri
N
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002038:Bungarotoxins / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D018716:Molecular Mimicry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011978:Receptors, Nicotinic / Q000737:chemistry / Q000378:metabolism; D020349:Surface Plasmon Resonance / Q000379:methods*
D002038:Bungarotoxins; D010455:Peptides; D011978:Receptors, Nicotinic