Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
5420960 | Solid State Nuclear Magnetic Resonance | 2006 | 8 Pages |
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.
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Authors
Régis D. Gougeon, Marc Reinholdt, L. Delmotte, Jocelyne Miehé-Brendlé, Philippe Jeandet,