A novel heterodimeric antimicrobial peptide from the tree‐frog Phyllomedusa distincta

FEBS Letters

Batista, Cesar V.F³  Scaloni, Andrea⁴  Silva, Lindomar R³  Bloch, Carlos¹  Dukor, Rina²  Rigden, Daniel J¹  Rodrigues Romero, Adela⁵  Sebben, Antonio³  Talamo, Fabio⁴ 

[1] EMBRAPA-Cenargen, P.O. Box 02372, Brasilia, DF 70849-970, Brazil;Vysis Inc., 3100 Woodcreek Drive, Downers Grove, IL 60515, USA;Institute of Biology, University of Brasilia, Brasilia, DF 70910-900, Brazil;IABBAM-Centro Internazionale Servizi di Spettrometria di Massa, Consiglio Nazionale delle Ricerche, via Argine 1085, 80147 Naples, Italy;Institute of Chemistry, National Autonomous University of Mexico-UNAM, Mexico City, Mexico

关键词: Antimicrobial peptide;    Disulphide;    Heterodimer;    Conformation analysis;    Phyllomedusa distincta;    CD;    circular dichroism;    ESMS;    electrospray mass spectrometry;    TFE;    2;    2;    2-trifluoroethanol;    FTIR;    Fourier-transformed infrared;    LUV;    large unilamellar vesicle;    MIC;    minimal inhibitory concentration;   

DOI  :  10.1016/S0014-5793(01)02324-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 β-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.

【 授权许可】

Unknown