| Autor: |
A G, Craig, E C, Jimenez, J, Dykert, D B, Nielsen, J, Gulyas, F C, Abogadie, J, Porter, J E, Rivier, L J, Cruz, B M, Olivera, J M, McIntosh |
| Rok vydání: |
1997 |
| Předmět: |
|
| Zdroj: |
The Journal of biological chemistry. 272(8) |
| ISSN: |
0021-9258 |
| Popis: |
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. The sequences of the two peptides and were determined using a combination of mass spectrometry, amino acid, and chemical sequence analyses, where Pca = pyroglutamic acid, Hyp = hydroxyproline, Gla = gamma-carboxyglutamate, and Trp* = L-6-bromotryptophan. The precise structure and stereochemistry of the modified residue were determined as L-6-bromotryptophan by synthesis, co-elution, and enzymatic hydrolysis experiments. To our knowledge this is the first documentation of tryptophan residues in peptides/proteins being modified in a eukaryotic system and the first report of halogenation of tryptophan in vivo. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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