Solid-state NMR investigation on the interactions between a synthetic montmorillonite and two homopolypeptides.

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…