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RESEARCH PRODUCT
Experimental and theoretical NMR studies of interaction between phenylalanine derivative and egg yolk lecithin
Tomasz PtakRoksana WałęsaMałgorzata A. BrodaTeobald KupkaDawid Siodłaksubject
Models Molecularfood.ingredientMagnetic Resonance SpectroscopyPhenylalanineMolecular ConformationPhenylalanineLecithinDFTchemistry.chemical_compoundfoodYolkLecithinsMaterials TestingOrganic chemistryAnimalsGeneral Materials ScienceComputer Simulationhydrogen bondChloroformBinding Sitesintermolecular interactionsHydrogen bondIntermolecular forceGeneral ChemistryCarbon-13 NMREgg YolkpeptideNMR3. Good healthCrystallographylecithinchemistryModels ChemicalChickensDerivative (chemistry)description
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2014-03-18 | Magnetic Resonance in Chemistry |