Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin

The interaction of phenylalanine diamide (Ac‐Phe‐NHMe) with egg yolk lecithin (EYL) in chloroform was studied by 1H and 13C 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 si...

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Published in:Magnetic resonance in chemistry 2014-06, Vol.52 (6), p.298-305
Main Authors: Wałęsa, Roksana, Ptak, Tomasz, Siodłak, Dawid, Kupka, Teobald, Broda, Małgorzata A.
Format: Article
Language:English
Subjects:
Animals
Binding Sites
Charging
Chickens
Chloroform
Computer Simulation
DFT
Egg Yolk - chemistry
hydrogen bond
intermolecular interactions
Lecithin
Lecithins - chemistry
Magnetic Resonance Spectroscopy - methods
Materials Testing
Mathematical analysis
Models, Chemical
Models, Molecular
Molecular Conformation
NMR
Nuclear magnetic resonance
peptide
Peptides
Phenylalanine
Phenylalanine - analysis
Phenylalanine - chemistry
Phosphates
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Summary:The interaction of phenylalanine diamide (Ac‐Phe‐NHMe) with egg yolk lecithin (EYL) in chloroform was studied by 1H and 13C 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. Copyright © 2014 John Wiley & Sons, Ltd. The interaction of phenylalanine diamide (Ac‐Phe‐NHMe) with egg yolk lecithin in chloroform was studied by NMR spectroscopy and theoretical calculations. Results of our study indicate that the interaction of peptides with lecithin occur 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.
ISSN:0749-1581
1097-458X
DOI:10.1002/mrc.4064