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Peptides as weapons against microorganisms in the chemical defense system of vertebrates.
This secondary, chemical immune system provides vertebrates with a repertoire of small peptides that are promptly synthesized upon induction, easily stored in large amounts, and readily available for antimicrobial warfare. Expand
Interaction of antimicrobial dermaseptin and its fluorescently labeled analogues with phospholipid membranes.
The results provide good correlation between the peptide's strong binding and its ability to permeate membranes composed of acidic phospholipids, as revealed by a dissipation of diffusion potential and a release of entrapped calcein from SUV. Expand
The vertebrate peptide antibiotics dermaseptins have overlapping structural features but target specific microorganisms.
Results suggest that, despite 40% sequence similarities, the dermaseptins have distinct spectra of anti-microbial activity and may act in concert to circumvent host invasion by providing frogs with a better shielding against a broad array of microorganisms. Expand
Selective Cytotoxicity of Dermaseptin S3 toward IntraerythrocyticPlasmodium falciparum and the Underlying Molecular Basis*
- J. K. Ghosh, D. Shaool, +5 authors A. Mor
- Biology, Medicine
- The Journal of Biological Chemistry
- 12 December 1997
A mechanism by which dermaseptins permeate cells and affect intraerythrocytic parasites is proposed, albeit with different kinetics. Expand
Improved antimicrobial peptides based on acyl-lysine oligomers
- I. Radzishevsky, S. Rotem, Dmitry Bourdetsky, S. Navon-Venezia, Y. Carmeli, A. Mor
- Chemistry, Medicine
- Nature Biotechnology
- 27 May 2007
We describe peptidomimetic oligomers that show rapid, nonhemolytic, broad-spectrum bactericidal properties in mice and do not induce the emergence of resistance. The oligomers contain acyl chains,… Expand
Spectrum of antimicrobial activity and assembly of dermaseptin-b and its precursor form in phospholipid membranes.
The exceptional property of DS-B to bind strongly to phospholipid membranes and to form small bundles correlates with its high potential to kill yeast and filamentous fungi. Expand
Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.
- A. Mor, V. Nguyen, A. Delfour, D. Migliore-Samour, P. Nicolas
- Chemistry, Medicine
- 10 September 1991
The synthetic replicate was shown to be indistinguishable from natural dermaseptin with respect to chromatographic properties, amino acid sequence determination, and mass spectrometry analysis. Expand
Isolation and structure of novel defensive peptides from frog skin.
The isolation and characterization of four novel antimicrobial peptides from frog skin through the combined use of an anti-dermaseptin enzyme immunoassay and an antifungal bioassay suggest that adenoregulin should be included in the dermase leptin family of peptides. Expand
The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity.
Dermaseptin-(1-18)-NH2 may be considered as a useful and highly tractable tool for identifying key features responsible for membrane permeabilization and as a starting point for the design of new therapeutic agents. Expand
Structure-Activity Relationship Study of Antimicrobial Dermaseptin S4 Showing the Consequences of Peptide Oligomerization on Selective Cytotoxicity*
The data indicated that N-terminal domain interaction between dermaseptin S4 monomers is responsible for the peptide's oligomerization in solution and, hence, for its limited spectrum of action. Expand