1H‐nmr studies of receptor‐selective substance P analogues reveal distinct predominant conformations in DMSO‐d6
作者:
Dina Levian‐Teitelbaum,
Nancy Kolodny,
Michael Chorev,
Zvi Selinger,
Chaim Gilon,
期刊:
Biopolymers
(WILEY Available online 1989)
卷期:
Volume 28,
issue 1
页码: 51-64
ISSN:0006-3525
年代: 1989
DOI:10.1002/bip.360280108
出版商: Wiley Subscription Services, Inc., A Wiley Company
数据来源: WILEY
摘要:
AbstractProton nmr parameters are reported for DMSO‐d6solutions of two receptor‐selective substance P analogues: Ac[Arg6, Pro9]SP6‐11, which is selective for the NK‐1 (SP‐P) receptor and [pGlu6, N‐MePhe8]SP6‐11, which selectively activates the NK‐3 (SP‐N) receptor. Full peak assignments of both analogues were obtained by COSY experiments. The chemical shifts, coupling constants, and temperature coefficients of amide proton chemical shifts as well as NOESY effects and calculated side‐chain rotamer populations of Phe side chains are reported for both peptides. Analysis of coupling constants and temperature coefficients together with the nuclear Overhauser enhancement spectroscopy effects suggest that Ac[Arg6, Pro9]SP6‐11has atransconfiguration about the Phe8‐Pro9amide bond and the preferred conformation of this analogue has a type I β‐turn. The nmr data for [pGlu6, N‐MePhe8]SP6‐11suggest that this peptide exists as a mixture ofcis–transisomers in which thecisisomer can preferably adopt a type VI β‐turn conformation, and thetransisomer can adopt a γ‐turn conformation. There are indications that the two last turns are stabilized by a hydrogen bond between thesyncarboxa
点击下载:
PDF
(812KB)
返 回