Wałęsa Roksana, Ptak Tomasz, Siodłak Dawid, Kupka Teobald, Broda Małgorzata A
Faculty of Chemistry, University of Opole, Oleska 48 Str., 45-052, Opole, Poland.
Magn Reson Chem. 2014 Jun;52(6):298-305. doi: 10.1002/mrc.4064. Epub 2014 Mar 18.
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.
通过¹H和¹³C核磁共振研究了苯丙氨酸二酰胺（Ac-Phe-NHMe）与氯仿中蛋黄卵磷脂（EYL）的相互作用。通过N-H···O或/和C-H···O氢键稳定的六种复合物EYL-Ac-Phe-NHMe在M06-2X/6-31G(d,p)水平上进行了优化。使用GIAO（含原子轨道规范）核磁共振计算在VSXC和B3LYP理论水平结合STO-3Gmag基组，支持了EYL和Ac-Phe-NHMe核磁共振信号的归属。我们的研究结果表明，肽与卵磷脂的相互作用主要发生在卵磷脂的极性“头部”。此外，与Ac-Phe-NHMe发生氢键相互作用最可能的卵磷脂位点是磷酸基团中带负电荷的氧，其作为质子受体。
