title: Magic angle spinning NMR study of interaction of N-terminal sequence of dermorphin (Tyr-d-Ala-Phe-Gly) with phospholipids.
abstract: Two modifications of the Tyr-d-Ala-Phe-Gly tetrapeptide with different C-terminal groups (Tyr-d-Ala-Phe-Gly-OH 1 and Tyr-d-Ala-Phe-Gly-NH(2)2) were investigated by various nuclear magnetic resonance sequences under magic angle spinning. The structural constraints obtained from the magic angle spinning nuclear magnetic resonance measurements suggest that both peptides are aligned on the surface of the membrane and that the sandwich-like π-CH(3)-π arrangement of the pharmacophore is preserved. The influence of the chemical modification of the C-terminal residue of 1 and 2 on their interaction with phosphate group of the phospholipid in the subgel phase L(c) and the conformation of the peptides in the liquid crystalline phase L(α) are discussed. The correlation between the X-ray structure of 1 in the solid state and 1 embedded into a membrane in the L(c) phase is presented on the basis of the comparative analysis of the two-dimensional (13)C-(13)C dipolar-assisted rotational resonance cross-peaks and the (13)C isotropic chemical shifts.
authors: Polish Academy of Sciences, Lodz, Poland.
authors: Agata
authors: A
authors: Jeziorna
authors: Tomasz
authors: T
authors: Pawlak
authors: Katarzyna
authors: K
authors: Trzeciak-Karlikowska
authors: Piotr
authors: P
authors: Paluch
authors: Marek J
authors: MJ
authors: Potrzebowski
mesh_terms: D008958:Models, Molecular; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D018847:Opioid Peptides / Q000737:chemistry*; D010743:Phospholipids / Q000737:chemistry*; D011487:Protein Conformation; D014961:X-Ray Diffraction
chemical_list: D018847:Opioid Peptides; D010743:Phospholipids; C030058:dermorphin