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-p
eptide recognition process. The conformation of substance P bound to vesicl
es consisting of perdeuterated phosphatidylcholine has been investigated by
means of two-dimensional transferred nuclear Overhauser (trNOE) spectrosco
py. Nuclear magnetic resonance data analysis resulted in a unique conformat
ional 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 mediu
m-range trNOE in the N-terminal part indicates its structural flexibility.
(C) 2000 John Wiley & Sons, Inc.