期刊
PEPTIDES
卷 41, 期 -, 页码 38-44出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2013.02.016
关键词
Conus cancellatus; Conus austini; Vermivorous; Conotoxin; Six Cys; Paralysis
资金
- NIH National Institute of General Medical Sciences [GM48677]
- Consejo Nacional de Ciencia y Tecnologia, Mexico (CONACYT) [30701-N, 41477-Q, 43754-Q]
- Programa de Apoyo a Proyectos de Investigacion e Innovacion Tecnologica, Universidad Nacional Autonoma de Mexico (PAPIIT-UNAM) [IN-204403]
- CONACYT [144622]
- Direccion General de Estudios de Posgrado, Universidad Nacional Autonoma de Mexico (DGEP-UNAM)
The present study details the purification, the amino acid sequence determination, and a preliminary characterization of the biological effects in mice of a new conotoxin from the venom of Conus cancellatus (jr. syn.: Conus austini), a worm-hunting cone snail collected in the western Gulf of Mexico (Mexico). The 23-amino acid peptide, called as25a, is characterized by the sequence pattern CX1CX2CX8CX1CCX5, which is, for conotoxins, a new arrangement of six cysteines (framework XXV) that form three disulfide bridges. The primary structure (CKCPSCNFNDVTENCKCCIFRQP*; *, amidated C-terminus; calculated monoisotopic mass, 2644.09 Da) was established by automated Edman degradation after reduction and alkylation, and MALDI-TOF and ESI mass spectrometry (monoisotopic mass, 2644.12/2644.08 Da). Upon intracranial injection in mice, the purified peptide provokes paralysis of the hind limbs and death with a dose of 240 pmol (similar to 0.635 mu g, similar to 24.9 ng/g). In addition, a post-translational variant of this peptide (as25b) was identified and determined to contain two hydroxyproline residues. These peptides may represent a novel conotoxin gene superfamily. (c) 2013 Elsevier Inc. All rights reserved.
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