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 Lettjournal_title
FEBS lettersauthors
Batista CV,Scaloni A,Rigden DJ,Silva LR,Rodrigues Romero A,Dukor R,Sebben A,Talamo F,Bloch Cdoi
10.1016/s0014-5793(01)02324-9keywords:
subject
Has Abstractpub_date
2001-04-06 00:00:00pages
85-9issue
1-2eissn
0014-5793issn
1873-3468pii
S0014-5793(01)02324-9journal_volume
494pub_type
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