Solution structure of nocistatin, a new peptide analgesic

Citation
O. Crescenzi et al., Solution structure of nocistatin, a new peptide analgesic, BIOPOLYMERS, 53(3), 2000, pp. 257-264
Citations number
45
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOPOLYMERS
ISSN journal
00063525 → ACNP
Volume
53
Issue
3
Year of publication
2000
Pages
257 - 264
Database
ISI
SICI code
0006-3525(200003)53:3<257:SSONAN>2.0.ZU;2-F
Abstract
Nocistatin, a new heytadecapeptide encoded in the bPNP-3 gene, has a powerf ul biological activity connected with the mechanisms of pain transmission. It does nor bind to the opioid receptors but to another brain receptor with high affinity. In order to substantiate these novel biological data with a structural basis, we have undertaken a conformational study in solution. P roton nmr data ill helicogenic solvents are consistent with a well-defined helical structure that is consistent with the nmr parameters of the the C-t erminal octapeptide, a shorter fragment that retains allodynin-blocking act ivity. (C) 2000 John Wiley & Sons, Inc.