A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea.

A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Research Abstract Details 

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A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Abstract Text:

Alan Hunter Thompson,Anthony John Bjourson,David Francis Orr,Chris Shaw,Stephen McClean,

Studies conducted on amphibian skin secretions over the past 40 years have isolated and identified huge arrays of bioactive peptides, many of which have demonstrated potent anti-microbial activity. Such peptides are attracting increasing attention due to the growing problem of pathogenic microorganisms resistant to conventional antibiotics. The current study utilized a combined proteomic/genomic approach to facilitate the high throughput sequencing of five novel dermaseptins and four novel phylloseptins from the skin secretions of Phyllomedusa hypochondrialis azurea. Peptides were partially identified using Q-TOF MS/MS fragmentation and de novo sequencing, while a cDNA library was constructed from the lyophilized skin secretion. 3'-RACE reactions used primers designed for the highly conserved 5'-signal regions of previously deduced dermaseptin precursors. cDNA sequenced peptides were attributed to their respective fragmentation spectra to confirm the structure of the final processed peptides. Such an approach identified post-translational modifications in addition to deciphering isobaric amino acids. Several of the peptides were purified to homogeneity and displayed potent antimicrobial activity with minimum inhibitory concentrations starting at 0.4 microM when tested against and range of Gram-positive and Gram-negative bacteria including Escherichia coli, Staphylococcus aureus and Micrococcus luteus.

A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Publishing Authors By Initials

AH Thompson,AJ Bjourson,DF Orr,C Shaw,S McClean,

For similar integumentary system: skin research abstracts see: integumentary system: skin research

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A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Peptides

VOLUME: 28

Page Numbers: 1331-43

Journal Abbreviation: Peptides

ISSN: 0196-9781

DAY: 10

MONTH: 05

YEAR: 2007

A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Information

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LANGUAGE: eng

NlmUniqueID: 8008690

A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Keywords Mesh Terms:

KEYWORDS: Skin

MESH TERMS: secretion

Chemical & Substance for Abstract: A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea. Information

Substance Name: dermaseptin

Registry Number: 136212-91-4

Grant and Affiliation Information for A combined mass spectrometric and cDNA sequencing approach to the isolation and characterization of novel antimicrobial peptides from the skin secretions of Phyllomedusa hypochondrialis azurea.

AFFILIATION: Institute of Biomedical Sciences, University of Ulster, Cromore Road, Coleraine, Co Londonderry BT52 1SA, Northern Ireland, UK.

Country: United States

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MEDLINETA: Peptides

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