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Molluscan neuropeptides

Y Yasuda-Kamatani1

  • 1Suntory Institute for Bioorganic Research, Osaka, Japan.

EXS
|February 9, 1999
PubMed
Summary
This summary is machine-generated.

Molluscan neuropeptides containing D-amino acids, like Achatin-I, exhibit unique muscle activities. Molecular studies reveal L-to-D amino acid conversion impacts neuropeptide function and structure.

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Area of Science:

  • Neuroscience
  • Peptide Chemistry
  • Molluscan Biology

Background:

  • Molluscs utilize neuropeptides for physiological regulation.
  • D-amino acid-containing neuropeptides are found in molluscs, but their functional significance is not fully understood.

Purpose of the Study:

  • To investigate the physiological activities of various D-amino acid-containing neuropeptides from molluscs.
  • To explore the role of L-to-D amino acid conversion in neuropeptide function.

Main Methods:

  • Electrophysiological and pharmacological assays on isolated muscles and neurons.
  • Molecular biological studies on peptide precursor processing and epimerization.

Main Results:

  • Achatin-I, fulicin, and fulyal (from Achatina) showed excitatory/modulatory effects on muscles and neurons, while their L-isomers were inactive.

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    • Conclusions:

    • D-amino acid incorporation significantly influences the biological activity of molluscan neuropeptides.
    • The conversion of L-amino acids to D-amino acids via epimerization is a key mechanism in generating functionally distinct neuropeptides in molluscs.
    • Peptide structure and stereochemistry are critical determinants of neuropeptide function in physiological processes.