Solid-state NMR investigation on the interactions between a synthetic montmorillonite and two homopolypeptides.
Interactions of two homopolypeptides (polylysine and polyglutamic acid) with a synthetic montmorillonite were studied by 1H MAS, 1H-27Al HETCOR and 1H-13C CP-MAS NMR experiments. 1H-27Al HETCOR with 1H spin-diffusion NMR appears to be a powerful probe for the identification of the polypeptide fragments, which interact with the montmorillonite interlayer surfaces. In particular, selective interactions were observed between the polypeptide side-chains and the montmorillonite octahedral aluminum atoms. 1H-13C CP-MAS NMR experiments were used to assess the dynamics of the two polypeptides through the measurement of the t(1/2) characteristic time of selected carbons. Results indicate that the local mobility of the side chains and their interaction with the montmorillonite layers depend on the nature of the adsorbed polypeptides.
Gougeon
Régis D
RD
Laboratoire d'Ingénierie Moléculaire et Sensorielle des Aliments et des Produits de Santé, UPRES EA 581, ENSBANA, Université de Bourgogne, 1 Esplanade Erasme, 21079 Dijon, France. regis.gougeon@u-bourgogne.fr
Reinholdt
Marc
M
Delmotte
L
L
Miehé-Brendlé
Jocelyne
J
Jeandet
Philippe
P
D001546:Bentonite / Q000032:analysis* / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D010455:Peptides / Q000032:analysis* / Q000737:chemistry*; D012987:Soil / Q000032:analysis*
D010455:Peptides; D012987:Soil; D001546:Bentonite