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Novel post-translational modification involving bromination of tryptophan: identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom
Craig, A. Grey; Jimenez, Elsie C.; Dykert, John; Nielsen, David B.; Gulyas, Joseph; Abogadie, Fe C.; Porter, John; Rivier, Jean E.; Cruz, Lourdes J.
citation_title
Novel post-translational modification involving bromination of tryptophan: identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom
citation_date
1997
Description
We report a novel post-translational modification involving halogenation of tryptophan in peptides recovered from the venom of carnivorous marine cone snails (Conus). The residue, L-6-bromotryptophan, was identified in the sequence of a heptapeptide, isolated from Conus imperialis, a worm-hunting cone. This peptide does not elicit gross behavioral symptoms when injected centrally or peripherally in mice. L-6-Bromotryptophan was also identified in a 33-amino acid peptide from Conus radiatus; this peptide has been shown to induce a sleep-like state in mice of all ages and is referred to as bromosleeper peptide.
Type
text;
citation_publisher
American Society for Biochemistry and Molecular Biology (ASBMB)
Craig, A. G., Jimenez, E. C., Dykert, J., Nielsen, D. B., Gulyas, J., Abogadie, F. C., Porter, J., Rivier, J. E., Cruz, L. J., Olivera, B. M. & McIntosh, J. M. (1997). Novel post-translational modification involving bromination of tryptophan: identification of the residue, L-6-bromotryptophan, in peptides from Conus imperialis and Conus radiatus venom. Journal Biological Chemistry, 272(8), 4689-98.
Rights Management
(c)American Society for Biochemistry and Molecular Biology (ASBMB) http://www.asbmb.org/
