Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.

@article{Mor1991IsolationAA,
  title={Isolation, amino acid sequence, and synthesis of dermaseptin, a novel antimicrobial peptide of amphibian skin.},
  author={A. Mor and V. Nguyen and A. Delfour and D. Migliore-Samour and P. Nicolas},
  journal={Biochemistry},
  year={1991},
  volume={30 36},
  pages={
          8824-30
        }
}
A 34-residue antimicrobial peptide named dermaseptin was purified to homogeneity from amphibian skin by a 3-step protocol involving molecular sieve filtration, ion-exchange chromatography, and reversed-phase high-performance liquid chromatography. The complete amino acid sequence of dermaseptin, ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ, was determined by automated Edman degradation of the peptide and of fragments generated by trypsin. Fast atom bombardment mass spectra of dermaseptin gave a… Expand
Structure, Synthesis, and Molecular Cloning of Dermaseptins B, a Family of Skin Peptide Antibiotics*
TLDR
The remarkable similarity found between prepro-proteins that encode end products with strikingly different sequences, conformations, biological activities and modes of action suggests that the corresponding genes have evolved through dissemination of a conserved “secretory cassette” exon. Expand
Structure, synthesis, and activity of dermaseptin b, a novel vertebrate defensive peptide from frog skin: relationship with adenoregulin.
TLDR
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
Synthesis, antimicrobial activity and gene structure of a novel member of the dermaseptin B family.
TLDR
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
Two Novel Dermaseptin-Like Antimicrobial Peptides with Anticancer Activities from the Skin Secretion of Pachymedusa dacnicolor
TLDR
The dermaseptin antimicrobial peptide family contains members of 27–34 amino acids in length that have been predominantly isolated from the skins/skin secretions of phyllomedusine leaf frogs and exhibited moderate to high inhibition against the growth of the tested microorganisms and cancer cell lines with low haemolytic activity. Expand
Dermaseptin-PH: A Novel Peptide with Antimicrobial and Anticancer Activities from the Skin Secretion of the South American Orange-Legged Leaf Frog, Pithecopus (Phyllomedusa) hypochondrialis
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A novel dermaseptin peptide is reported, from the South American orange-legged leaf frogs, Pithecopus (Phyllomedusa) hypochondrialis, processing the shortest peptide length, namely Dermaseptin-PH, which shows a broad-spectrum of anticancer activities against several cancer cell lines. Expand
Phylloxin, a novel peptide antibiotic of the dermaseptin family of antimicrobial/opioid peptide precursors.
TLDR
The isolation, synthesis and cloning of phylloxin is described, a prototypical member of a novel family of antimicrobial peptides derived from the processing of a dermaseptin/dermorphin-like precursor. Expand
Biological Activities of Cationicity-Enhanced and Hydrophobicity-Optimized Analogues of an Antimicrobial Peptide, Dermaseptin-PS3, from the Skin Secretion of Phyllomedusa sauvagii
TLDR
The skin secretions of the subfamily Phyllomedusinae have long been known to contain a number of compounds with antimicrobial potential, and a biosynthetic dermaseptin-precursor cDNA was obtained from a skin secretion-derived cDNA library, and thereafter, the presence of the mature peptide was confirmed. Expand
Conformation–activity relationship of a novel peptide antibiotic: Structural characterization of dermaseptin DS 01 in media that mimic the membrane environment
TLDR
A new dermaseptin, named DS 01, from the skin secretion of Phyllomedusa oreades, showed not only strong antibacterial properties against Gram‐positive and Gram‐negative bacteria but also antiprotozoan activity in the μM range. Expand
Evaluating the Bioactivity of a Novel Antimicrobial and Anticancer Peptide, Dermaseptin-PS4(Der-PS4), from the Skin Secretion of Phyllomedusa sauvagii
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A novel dermaseptin peptide named Der-PS4 was discovered from the skin secretion of the waxy monkey tree frog, Phyllomedusa sauvagii, displaying a broad spectrum of antimicrobial activities against tested pathogenic microorganisms, however, exhibiting slight membrane-damaging effectiveness towards horse red blood cells. Expand
Isolation and structure of novel defensive peptides from frog skin.
TLDR
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
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A specific enzyme immunoassay is developed and synthetic peptides are used to detect and purify the new predicted heptapeptide 2.0, a novel D‐amino acid containing peptide that is named dermenkephalin because of its origin and its δ‐opioid activity and specificity. Expand
Identification of a D-alanine-containing polypeptide precursor for the peptide opioid, dermorphin.
TLDR
These observations confirm that, despite the presence of D-amino acid residues, dermorphin and dermenkephalin are genuine products of post-translational processing of a ribosomally made precursor and suggest that D-Ala and D-Met develop from a dehydrogenation/hydrogenation stereoinversion of their corresponding L isomers incorporated into pro-dermorphin. Expand
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Skin secretions from the South African frog Xenopus laevis have been chromatographed by high performance liquid chromatography, fractionated, and analyzed by fast atom bombardment-mass spectrometry (FAB-MS), suggesting that many of these skin secretions were peptides originating from additional processing of the xenopsin, caerulein, and PGLa precursors. Expand
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A family of peptides with broad-spectrum antimicrobial activity has been isolated from the skin of the African clawed frog Xenopus laevis and appears to represent a previously unrecognized class of vertebrate antimicrobial activities. Expand
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Two variants of this peptide have now been synthesized containing either L- or D-methionine as the second amino acid, exhibiting high-affinity and selectivity for delta opioid receptors in the mouse vas deferens and in rat brain homogenates. Expand
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TLDR
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TLDR
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