L−Lysine Amino Acid Adsorption on Zeolite L: a Combined Synchrotron, X‐Ray and Neutron Diffraction Study
Dr. Giada Beltrami,
Prof. Annalisa Martucci,
Prof. Luisa Pasti,
Dr. Tatiana Chenet,
Dr. Matteo Ardit,
Dr. Lara Gigli,
Dr. Mirco Cescon,
Dr. Emmanuelle Suard
Affiliations
Dr. Giada Beltrami
Department of Physics and Earth Sciences University of Ferrara Via Saragat 1 44121 Ferrara Italy
Prof. Annalisa Martucci
Department of Physics and Earth Sciences University of Ferrara Via Saragat 1 44121 Ferrara Italy
Prof. Luisa Pasti
Dipartimento di Scienze Chimiche e Farmaceutiche University of Ferrara Via Fossato di Mortara 17 44121 Ferrara Italy
Dr. Tatiana Chenet
Dipartimento di Scienze Chimiche e Farmaceutiche University of Ferrara Via Fossato di Mortara 17 44121 Ferrara Italy
Dr. Matteo Ardit
Department of Physics and Earth Sciences University of Ferrara Via Saragat 1 44121 Ferrara Italy
Dr. Lara Gigli
Elettra-Sincrotrone Trieste S.C.p.A. Materials Characterisation by X-ray diffraction (MCX) beamline Strada Statale 14 - km 163,5 in AREA Science Park Basovizza Trieste Italy
Dr. Mirco Cescon
Dipartimento di Scienze Chimiche e Farmaceutiche University of Ferrara Via Fossato di Mortara 17 44121 Ferrara Italy
Dr. Emmanuelle Suard
Institute Max Von Laue and Paul Langevin, D2B beamline BP156 38042 Grenoble France
Abstract Combined neutron and X‐ray powder diffraction techniques highlighted the sorption capacity of the acidic L zeolite towards the L‐lysine amino acid. The role of zeolite channels in the stabilization of the lysine absorbed and the effect of water on protein structure are elucidated at atomistic level. The stabilization of the L α‐helical conformation is related to strong H‐bonds between the tail aminogroups of lysine molecules and the Brønsted acid site as well as to complex intermolecular H‐bond system between water molecules, zeolite and amino acid. This finding is relevant in the catalytic synthesis of polypeptide, as well as in industrial biotechnology by qualitatively predicting binding behaviour
