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Peptidomic analysis of the skin secretions of the frog Pachymedusa dacnicolor

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Abstract

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.

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Acknowledgments

This research was supported by grant from the Dirección General de Asuntos del Personal Académico (DGAPA) of the National Autonomous University of Mexico-UNAM (Grant number IN221508 to CVFB).

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Correspondence to Cesar Vicente Ferreira Batista.

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Meneses, E.P., Villa-Hernández, O., Hernández-Orihuela, L. et al. Peptidomic analysis of the skin secretions of the frog Pachymedusa dacnicolor . Amino Acids 40, 113–122 (2011). https://doi.org/10.1007/s00726-010-0564-9

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  • DOI: https://doi.org/10.1007/s00726-010-0564-9

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