A biologically active hydrophobic T-1-conotoxin from the venom of Conus spurius.
Peptides
; 27(3): 500-5, 2006 Mar.
Article
em En
| MEDLINE
| ID: mdl-16297502
ABSTRACT
A major, very hydrophobic peptide, sr5a, was purified from the venom duct of Conus spurius specimens collected in the Yucatan Channel, Mexico. Its amino acid sequence (IINWCCLIFYQCC; calculated monoisotopic mass assuming two disulfide bridges 1616.68 Da) was determined by automatic Edman degradation after reduction and alkylation, and confirmed by mass spectrometry (ESI monoisotopic mass, 1616.60; MALDI monoisotopic mass 1616.42 Da). The primary structure of sr5a showed the pattern that characterizes the family of the T-1-conotoxins, which belong to the T-superfamily of conotoxins. The disulfide bonds were determined by partial reduction and alkylation with N-ethylmaleimide, followed by total reduction and alkylation with 4-vinylpyridine, and automatic Edman sequencing. The connectivity of the Cys residues (I-III, II-IV) is the same as that found in the T-1-conotoxin family. When injected intracranially (2.0 nmol) into mice, peptide sr5a caused depressed behavioral activity.
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Base de dados:
MEDLINE
Assunto principal:
Peptídeos Cíclicos
/
Conotoxinas
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article