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Amphibian Skin Secretomics: Application of Parallel Quadrupole Time-of-Flight Mass Spectrometry and Peptide Precursor cDNA Cloning to Rapidly Characterize the Skin Secretory Peptidome of Phyllomedusa hypochondrialis azurea: Discovery of a Novel Peptide Family, the Hyposins
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Abstract

This study reports the variety of peptides present in the skin secretory peptidome of Phyllomedusa hypochondrialis azurea. Peptide structures, along with post-translational modifications, were elucidated by QTOF MS/MS analysis, cDNA sequencing, or a combination of both. Twenty-two peptides, including 19 novel structures, were identified from six different structural classes, including tryptophyllins, dermorphins, and a novel group of peptides termed hyposins. The study demonstrates the power of this combined approach to mine the rich peptidome compliment of the amphibian defensive skin secretome.
Keywords: amphiban skin • secretome • host defense • hyposin • mass spectrometry • de novo sequencing • Phyllomedusa hypochondrialis azurea
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This article has been cited by 1 ACS Journal articles (1 most recent appear below).

Experimental Approach for Deep Proteome Measurements from Small-Scale Microbial Biomass Samples
Melissa R. Thompson, Karuna Chourey, Jennifer M. Froelich, Brian K. Erickson, Nathan C. VerBerkmoes and Robert L. HettichAnalytical Chemistry2008 80 (24), 9517-9525Experimental Approach for Deep Proteome Measurements from Small-Scale Microbial Biomass Samples
Melissa R. Thompson, Karuna Chourey, Jennifer M. Froelich, Brian K. Erickson, Nathan C. VerBerkmoes and Robert L. HettichAnalytical Chemistry2008 80 (24), 9517-9525Many methods of microbial proteome characterizations require large quantities of cellular biomass (>1−2 g) for sample preparation and protein identification. Our experimental approach differs from traditional techniques by providing the ability to ...
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History
- Published In Issue September 07, 2007
- Received May 9, 2007
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