|
|||||
|
|
Solid-state NMR investigation on the interactions between a synthetic montmorillonite and two homopolypeptides |
|
| Authors: | Gougeon Régis D Reinholdt Marc Delmotte L Miehé-Brendlé Jocelyne Jeandet Philippe |
| Institution: | aLaboratoire 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 bInstitut Universitaire de la Vigne et du Vin, Université de Bourgogne, Rue Claude Ladrey, BP 27877, 21078 Dijon, France cDepartment of Geology, University of Illinois at Urbana-Champaign, 1301 West Green Street, Urbana, IL 61801, USA dLaboratoire de Matériaux à Porosité Contrôlée, Université de Haute Alsace, UMR-CNRS 7016, 3, Rue A. Werner, 68093 Mulhouse Cedex, France eLaboratoire d’Oenologie et de Chimie Appliquée U.R.V.V.C. UPRES EA 2069, Université de Reims, Faculté des Sciences, Moulin de la Housse, BP 1039, 51687 Reims Cedex 2, France |
| Abstract: | 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 t1/2 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. |
| Keywords: | Montmorillonite Polypeptides Solid-state NMR Interface Dynamics |
| 本文献已被 ScienceDirect PubMed 等数据库收录！ | |