2001
DOI: 10.1016/s0014-5793(01)02324-9
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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 treefrog 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… Show more

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Cited by 76 publications
(63 citation statements)
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“…4, which is published as supporting information on the PNAS web site). Furthermore, CD analysis of natural and synthetic D1 in water and trifluoroethanol afforded spectra almost undistinguishable and fully superimposable to those already reported (7), suggesting that the two peptides adopted an identical conformation in the same solvents.…”
Section: Resultssupporting
confidence: 68%
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“…4, which is published as supporting information on the PNAS web site). Furthermore, CD analysis of natural and synthetic D1 in water and trifluoroethanol afforded spectra almost undistinguishable and fully superimposable to those already reported (7), suggesting that the two peptides adopted an identical conformation in the same solvents.…”
Section: Resultssupporting
confidence: 68%
“…The possibility that chains A and B should maintain a helical conformation after membrane interaction was strongly suggested by CD spectroscopy analysis, demonstrating an increase in helical content on passing from an aqueous to a hydrophobic͞membrane-mimetic environment (Fig. 4 and data not shown) (7). Accordingly, D1 appears to have all of the structural features to insert and form pores in membranes by autoassociation of different molecules.…”
Section: Discussionmentioning
confidence: 95%
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“…burmeisteri skin secretion, of two peptide precursor-encoding cDNAs and their encoded peptides which are homologous to chains A and B from the heterodimeric peptide, distinctin, originally isolated from the skin of the related specie, P. distincta [10]. Differential analysis of native and reductively-alkylated P. burmeisteri distictin demonstrated that the intermolecular disulfide bridge between both chains is an endogenous and specific posttranslational modification (PTM).…”
Section: Accepted M Manuscriptmentioning
confidence: 99%
“…A family of AMPs (amolopin) with unique sequence (NILSSIVNGINRALSFFG) is found in the torrent frog, A. loloensis (45). In addition, in skin secretions of frog Phyllomedusa distincta, a particular heterodimer AMP with two peptide chains linked by disulfide bonds is also discovered (75).…”
Section: Secondary Structure Of Antimicrobial Peptidesmentioning
confidence: 99%