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Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin
Author(s) -
Wałęsa Roksana,
Ptak Tomasz,
Siodłak Dawid,
Kupka Teobald,
Broda Małgorzata A.
Publication year - 2014
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.4064
Subject(s) - chemistry , lecithin , hydrogen bond , proton nmr , phenylalanine , proton , yolk , computational chemistry , stereochemistry , crystallography , molecule , organic chemistry , chromatography , amino acid , biochemistry , physics , food science , quantum mechanics
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‐3G mag 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. Copyright © 2014 John Wiley & Sons, Ltd.