A novel heterodimeric antimicrobial peptide from the tree-frog Phyllomedusa distincta.

Abstract:

:We present here the purification and the analysis of the structural and functional properties of distinctin, a 5.4 kDa heterodimeric peptide with antimicrobial activity from the tree-frog Phyllomedusa distincta. This peptide was isolated from the crude extract of skin granular glands by different chromatographic steps. Its minimal inhibitory concentration was determined against pathogenic Escherichia coli, Staphylococcus aureus, Enterococcus faecalis and Pseudomonas aeruginosa strains. Amino acid sequencing and mass spectrometric investigations demonstrated that distinctin is constituted of two different polypeptide chains connected by an intermolecular disulphide bridge. Circular dichroism and Fourier-transformed infrared spectroscopy studies showed that this molecule adopts, in water, a structure containing a significant percentage of anti-parallel beta-sheet. A conformational variation was observed under experimental conditions mimicking a membrane-like environment. Database searches did not show sequence similarities with any known antimicrobial peptides. In the light of these results, we can consider distinctin as the first example of a new class of antimicrobial heterodimeric peptides from frog skin.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Batista CV,Scaloni A,Rigden DJ,Silva LR,Rodrigues Romero A,Dukor R,Sebben A,Talamo F,Bloch C

doi

10.1016/s0014-5793(01)02324-9

keywords:

subject

Has Abstract

pub_date

2001-04-06 00:00:00

pages

85-9

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(01)02324-9

journal_volume

494

pub_type

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