Spatial structures of the bradykinin potentiating peptide F from Agkistrodon piscivorus piscivoris venom

Bradykinin potentiating peptides usually show two different activities, potentiation of bradykinin and inhibition of angiotensin converting enzyme (ACE). Exceptions of this rule have been found suggesting that both effects occur independently. This study of peptide F by means of NMR spectroscopy sho...

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Veröffentlicht in:	Toxicon (Oxford) 1999-04, Vol.37 (4), p.661-676
Hauptverfasser:	Faria Ferreira, L.A, Auer, H, Haslinger, E, Fedele, Chr, Habermehl, G.G
Format:	Artikel
Sprache:	eng
Schlagworte:	Agkistrodon - metabolism Agkistrodon piscivorus piscivorus Animal poisons toxicology. Antivenoms Animals Biological and medical sciences Bradykinin - pharmacology Chromatography, High Pressure Liquid Drug Synergism Electrophoresis, Capillary Enkephalin, Methionine - analogs & derivatives Enkephalin, Methionine - chemistry Enkephalin, Methionine - pharmacology Magnetic Resonance Spectroscopy Mass Spectrometry Medical sciences Molecular Conformation Molecular Structure Proline - chemistry Protein Precursors - chemistry Protein Precursors - pharmacology Snake Venoms - chemistry Toxicology
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Zusammenfassung:	Bradykinin potentiating peptides usually show two different activities, potentiation of bradykinin and inhibition of angiotensin converting enzyme (ACE). Exceptions of this rule have been found suggesting that both effects occur independently. This study of peptide F by means of NMR spectroscopy shows clearly two different main conformations of the molecule. These different conformations may be the reason for the different activities.
ISSN:	0041-0101 1879-3150
DOI:	10.1016/S0041-0101(98)00208-6