The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity.

  title={The NH2-terminal alpha-helical domain 1-18 of dermaseptin is responsible for antimicrobial activity.},
  author={A. Mor and P. Nicolas},
  journal={The Journal of biological chemistry},
  volume={269 3},
  • A. Mor, P. Nicolas
  • Published 1994
  • Biology, Medicine
  • The Journal of biological chemistry
Dermaseptin, a 34-amino acid residue cationic peptide, was recently shown to inhibit the growth of pathogenic fungi responsible for severe opportunistic infections accompanying immunodeficiency syndrome and the use of immunosuppressive agents. To improve our understanding of the mechanism by which dermaseptin exerts its potent antimicrobial action, a series of either NH2- or COOH-terminally truncated analogs was synthesized. These analogs were evaluated for their ability to inhibit the growth… Expand
Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin.
The observation that adenoregulin enhances binding of agonists to the adenosine receptor may in fact be a consequence of its ability to alter the structure of biological membranes and to produce signal transduction via interactions with the lipid bilayer, bypassing cell surface receptor interactions. Expand
Mechanism of antibacterial action of dermaseptin B2: interplay between helix-hinge-helix structure and membrane curvature strain.
The results indicate that Drs B2 induces a strong perturbation of anionic lipid bilayers, resides at the hydrocarbon core-water interface, parallel to the plane of the membrane, and interacts preferentially with the polar head groups and glycerol backbone region of the anionic phospholipids, as well as the region ofthe lipid acyl chain near the bilayer surface. Expand
Synthesis, antimicrobial activity and gene structure of a novel member of the dermaseptin B family.
Analysis of the cDNAs coding precursors for several opioid and antimicrobial peptides originating from the skin of various amphibian species revealed that the 25-residue preproregion of these preproforms are all encoded by conserved nucleotides encompassed by the first coding exon of the Drg3 gene. Expand
CHAPTER 45 – The Dermaseptins
The dermaseptins are a superfamily of gene-encoded host defense peptides that are produced by the skin of frogs belonging to the family Hylidae and most of these peptides are lethal against Grampositive and Gram-negative bacteria, yeasts, protozoan, fungi, and enveloped viruses, without harmful effect on mammalian cells. Expand
Inhibitory Action of a Truncated Derivative of the Amphibian Skin Peptide Dermaseptin s3 on Saccharomyces cerevisiae
A derivative of a natural antimicrobial peptide has potential, either alone or in combination with mild heating, to prevent the growth of or kill spoilage yeast. Expand
Antibacterial and leishmanicidal activities of temporin-SHd, a 17-residue long membrane-damaging peptide.
It is demonstrated that temporin-SHd, a 17-residue peptide with a net charge of +2 (FLPAALAGIGGILGKLF(amide), expressed a broad spectrum of antimicrobial activity. Expand
In vitro discriminative antipseudomonal properties resulting from acyl substitution of N-terminal sequence of dermaseptin s4 derivatives.
Various mechanistic studies failed to detect significant differences in secondary structure, bactericidal kinetics, or ability to perturb the cytoplasmic membrane, pointing to a similar mode of action. Expand
Dermaseptins as potential antirabies compounds.
This study highlights the potential interest of dermaseptins as non-expansive alternatives to rabies immunoglobulins for the treatment of rabies that continues to claim about 60,000 human lives per year worldwide, almost exclusively in developing countries. Expand
Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II.
The results demonstrate clearly that the proline hinge is responsible for the cell-penetrating ability of buforin II, and thecell- penetrating efficiency determines the antimicrobial potency of the peptide. Expand
Temporin-SHf, a New Type of Phe-rich and Hydrophobic Ultrashort Antimicrobial Peptide*
The short length, compositional simplicity, and broad-spectrum activity of temporin-SHf make it an attractive candidate to develop new antibiotic agents. Expand


ACS Symp . Ser : 222 - 235 ( 1991 )
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  • 1991