Peptidomic analysis of the skin secretions of the frog Pachymedusa dacnicolor

High-resolution mass spectrometry-based peptidomics has been used to characterize several components in electro-stimulated skin secretions of the endemic Mexican frog Pachymedusa dacnicolor. Peptide mass screening performed in an Orbitrap-XL mass spectrometer showed that P. dacnicolor skin secretion...

Full description

Saved in:
Bibliographic Details
Published in:Amino acids 2011, Vol.40 (1), p.113-122
Main Authors: Meneses, Erika P, Villa-Hernández, Oscar, Hernández-Orihuela, Lorena, Castro-Franco, Ruben, Pando, Victoria, Aguilar, Manuel B, Batista, Cesar Vicente Ferreira
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino acids
Analytical Chemistry
Animals
Anti-Bacterial Agents - chemistry
Anti-Bacterial Agents - metabolism
Antibacterial peptides
Antiinfectives and antibacterials
Anura - metabolism
Bacteria
Bacteria - drug effects
Biochemical Engineering
Biochemistry
Biomedical and Life Sciences
Escherichia coli
Frog skin
Frogs
Life Sciences
Mass spectrometers
Mass Spectrometry
Molecular Sequence Data
Molecular Weight
Neurobiology
Original Article
Peptide Mapping
Peptides
Peptidomics
Proteomics
Secretions
Sequence Alignment
Skin - chemistry
Skin - secretion
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:High-resolution mass spectrometry-based peptidomics has been used to characterize several components in electro-stimulated skin secretions of the endemic Mexican frog Pachymedusa dacnicolor. Peptide mass screening performed in an Orbitrap-XL mass spectrometer showed that P. dacnicolor skin secretions possess 194 different components with molecular masses ranging mainly from 500 to 6,000 Da. Dozens of molecules were partially sequenced including two novel protease inhibitors. Additionally, one posttranslationally modified bradykinin and two novel dermaseptin-like antimicrobial peptides were fully sequenced. The novel peptide named here DMS-DA5 was fully characterized and showed potent antibacterial activity against various bacteria such as Escherichia coli, Bacillus subtilis, Salmonella enterica serovar typhimurium, and Pseudomonas aeruginosa with minimal inhibitory concentrations from 3.10 to 25.0 μM.
ISSN:0939-4451
1438-2199
DOI:10.1007/s00726-010-0564-9