Proton magnetic resonance studies on dermorphin and its peptide fragments
1984; Wiley; Volume: 23; Issue: 11 Linguagem: Inglês
10.1002/bip.360231116
ISSN1097-0282
AutoresAnnalisa Pastore, Piero Andrea Temussi, Teodorico Tancredi, Severo Salvadori, Roberto Tomatis,
Tópico(s)Biochemical and Structural Characterization
ResumoAbstract Dermorphin (Tyr D ‐AlaPheGlyTyrProSerNH 2 ), a potent natural peptide opioid, its synthetic L‐Ala 2 analog, and all the N fragments from the tripeptide (Tyr D ‐AlaPheNH 2 ) to the parent hexapeptide amide were characterized for the first time by means of proton nmr spectroscopy at 11.74 T. Assignments of most protons of dermorphin were facilitated by the study of the N‐terminal fragments. Comparison of spectroscopic parameters with relative pharmacological activity is proposed as a possible means of studying flexible agonists in solution.
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