Solution structure of nocistatin, a new peptide analgesic

✍ Scribed by Orlando Crescenzi; Remo Guerrini; Delia Picone; Severo Salvadori; Teodorico Tancredi; Piero Andrea Temussi

• Publisher: Wiley (John Wiley & Sons)
• Year: 2000
• Tongue: English
• Weight: 139 KB
• Volume: 53
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/(sici)1097-0282(200003)53:3<257::aid-bip5>3.0.co;2-l

✦ Synopsis

Nocistatin, a new heptadecapeptide encoded in the bPNP-3 gene, has a powerful biological activity connected with the mechanisms of pain transmission. It does not 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. Proton nmr data in helicogenic solvents are consistent with a well-defined helical structure that is consistent with the nmr parameters of the C-terminal octapeptide, a shorter fragment that retains allodynia-blocking activity.