Isolation of L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide), a sea anemone neuropeptide containing an unusual amino-terminal blocking group

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Using a radioimmunoassay for the carboxyl-terminal sequence Arg-Asn-NH2, we have purified a peptide from acetic acid extracts of the sea anemone Anthopleura elegantissima. By classical amino acid analyses, mass spectrometry, and 1H NMR spectroscopy, the structure of this peptide was determined as 3-phenyllactyl-Leu-Arg-Asn-NH2. By using reversed-phase HPLC and a chiral mobile phase, it was shown that the 3-phenyllactyl group had the L configuration. Immunocytochemical staining with antiserum against Arg-Asn-NH2 showed that L-3-phenyllactyl-Leu-Arg-Asn-NH2 (Antho-RNamide) was localized in neurons of sea anemones. The L-3-phenyllactyl group has not been found earlier in neuropeptides of vertebrates or higher invertebrates. We propose that this residue renders Antho-RNamide resistant to nonspecific aminopeptidases, thereby increasing the stability of the peptide after neuronal release.
Original languageEnglish
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number14
Pages (from-to)5410-4
Number of pages5
ISSN0027-8424
Publication statusPublished - 1 Jul 1990

    Research areas

  • Amino Acid Sequence, Animals, Antibody Specificity, Chromatography, High Pressure Liquid, Chromatography, Ion Exchange, Cnidaria, Mass Spectrometry, Molecular Sequence Data, Neuropeptides, Oligopeptides, Radioimmunoassay, Sea Anemones, Sequence Homology, Nucleic Acid, Species Specificity

ID: 33514272