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  • Title: Comparative potency of some extended peptide chain members of the RFamide neuropeptide family, assessed on the hearts of Busycon canaliculatum and Buccinum undatum.
    Author: Moulis A, Huddart H, Hill RB.
    Journal: J Comp Physiol B; 2003 Nov; 173(8):637-42. PubMed ID: 12937940.
    Abstract:
    Twenty different RFamide neuropeptide analogues were examined for their relative potencies on the ventricles of Busycon canaliculatum and Buccinum undatum and on the atrium of Busycon to determine the essential requirements for activity at the RFamide receptor. None of the neuropeptide studies was inhibitory to natural cardiac rhythmicity or to FMRFamide (Phe-Met-Arg-Phe-NH(2)) or FLRFamide (Phe-Leu-Arg-Phe-NH(2)) responses. Two tripeptides studied were completely without effect, indicating that a minimum of four amino acids in the peptide chain length was essential for any activity. The original parent tetrapeptide FMRFamide was surprisingly less potent than many of the extended chain peptides such as the penta, hepta and decapeptides. These RFamide neuropeptides were strongly inotropic on both ventricles and the atrium, while on the latter they were strongly chronotropic despite several of these peptides being of a non-molluscan origin. Chain length seems to be of little importance for activity at the receptor. Surprisingly, SCP(B) (small cardioactive Peptide B) was not very effective in either Busycon or Buccinum ventricle. What was also clear was that the configuration of the carboxyl terminal was important for activity. Two neuropeptides in this study possessed an Arg-Met carboxyl terminal and were much less effective than FMRFamide, suggesting that an Arg-Phe terminal is most effective in receptor activation.
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