Structure-activity relations of the molluscan neuropeptide FMRFamide on some molluscan muscles |
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Authors: | S.D. Painter J.S. Morley David A. Price |
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Affiliation: | 1. Department of Biological Sciences, Florida State University, Tallahassee, Florida 32306, U.S.A.;2. Imperial Chemical Industries, Ltd., Pharmaceuticals Division, Alderley Park, Macclesfield, United Kingdom |
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Abstract: | Analogs of the molluscan neuropeptide FMRFamide were tested on four different molluscan muscle preparations which show qualitatively different responses to the peptide; the structure-activity relations are basically similar, but not identical. The C-terminal amide and the Arg3 residue are critical for FMRFamide-like activity on all four preparations. In contrast, analogs extended at the N-terminal or with conservative substitutions for the Phe1 or Met2 residue are approximately equipotent to FMRFamide. These structural requirements parallel those for the C-terminal tetrapeptide amide of gastrin. |
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