Characterization of substance P-membrane interaction by transferred nuclear Overhauser effect

Substance P, one of the mammalian tachykinins, is known to interact strongly with lipid bilayers and this interaction may play a role in the receptor–peptide recognition process. The conformation of substance P bound to vesicles consisting of perdeuterated phosphatidylcholine has been investigated by means of two‐dimensional transferred nuclear Overhauser (trNOE) spectroscopy. Nuclear magnetic resonance data analysis resulted in a unique conformational family characterized by a well‐defined conformation of the last seven C‐terminal amino acids, which consists of a sequence of nonstandard turns following each other in a helix‐like manner. The absence of short‐ or medium‐range trNOE in the N‐terminal part indicates its structural flexibility. © 2000 John Wiley & Sons, Inc. Biopoly 54: 297–306, 2000