Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin
Copyright © 2014 John Wiley & Sons, Ltd.
| Publié dans: | Magnetic resonance in chemistry : MRC. - 1985. - 52(2014), 6 vom: 17. Juni, Seite 298-305 |
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| Auteur principal: | |
| Autres auteurs: | , , , |
| Format: | Article en ligne |
| Langue: | English |
| Publié: |
2014
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| Accès à la collection: | Magnetic resonance in chemistry : MRC |
| Sujets: | Journal Article Research Support, Non-U.S. Gov't DFT NMR hydrogen bond intermolecular interactions lecithin peptide Lecithins Phenylalanine |
| Résumé: | Copyright © 2014 John Wiley & Sons, Ltd. The interaction of phenylalanine diamide (Ac-Phe-NHMe) with egg yolk lecithin (EYL) in chloroform was studied by (1)H and (13)C NMR. Six complexes EYL-Ac-Phe-NHMe, stabilized by N-H···O or/and C-H···O hydrogen bonds, were optimized at M06-2X/6-31G(d,p) level. The assignment of EYL and Ac-Phe-NHMe NMR signals was supported using GIAO (gauge including atomic orbital) NMR calculations at VSXC and B3LYP level of theory combined with STO-3Gmag basis set. Results of our study indicate that the interaction of peptides with lecithin occurs mainly in the polar 'head' of the lecithin. Additionally, the most probable lecithin site of H-bond interaction with Ac-Phe-NHMe is the negatively charged oxygen in phosphate group that acts as proton acceptor |
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| Description: | Date Completed 17.04.2015 Date Revised 12.05.2014 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1097-458X |
| DOI: | 10.1002/mrc.4064 |