Journal ArticleDOI
Antimicrobial peptides from the Brazilian frog Phyllomedusa distincta.
Cesar Vicente Ferreira Batista,Cesar Vicente Ferreira Batista,L Rosendo da Silva,Antonio Sebben,Andrea Scaloni,Lino Ferrara,G.R Paiva,T Olamendi–Portugal,Lourival D. Possani,Carlos Bloch +9 more
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TLDR
Different peptides were purified by chromatographic procedures from the skin-secretory glands of the frog Phyllomedusa distincta and showed potent antimicrobial activity against Gram-negative and Gram-positive bacteria.About:
This article is published in Peptides.The article was published on 1999-08-01. It has received 52 citations till now. The article focuses on the topics: Phyllomedusa distincta & Edman degradation.read more
Citations
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Journal ArticleDOI
The chemistry and biological activities of peptides from amphibian skin secretions.
Xueqing Xu,Ren Lai +1 more
Journal ArticleDOI
Host-defence peptides from the glandular secretions of amphibians: structure and activity
TL;DR: This review covers the literature on the subject of biologically active peptide from the glands of amphibians, which include neuropeptides, antimicrobial and anticancer active peptides, antiviral agents, fungicides and peptides which complex with Ca2+ calmodulin.
Journal ArticleDOI
Characterization of unique amphipathic antimicrobial peptides from venom of the scorpion Pandinus imperator.
Gerardo Corzo,Pierre Escoubas,Elba Villegas,Kevin J. Barnham,Weilan He,Raymond S. Norton,Terumi Nakajima +6 more
TL;DR: The first report of magainin-type polycationic antimicrobial peptides in scorpion venom is reported, which brings new insights into the mode of action of scorpions venom and also opens new avenues for the discovery of novel antibiotic molecules from arthropod venoms.
Journal ArticleDOI
The dermaseptin superfamily: a gene-based combinatorial library of antimicrobial peptides.
TL;DR: The molecular mechanisms leading to these vast combinatorial peptide libraries, and structural and functional properties of antimicrobial peptides of the dermaseptin and plasticin families, as well as those of dermasesptin S9, an amyloidogenic peptide with antimicrobial and chemoattractant activities are reviewed.
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Oxyopinins, Large Amphipathic Peptides Isolated from the Venom of the Wolf Spider Oxyopes kitabensis with Cytolytic Properties and Positive Insecticidal Cooperativity with Spider Neurotoxins
Gerardo Corzo,Elba Villegas,Froylan Gómez-Lagunas,Lourival D. Possani,Belokoneva Os,Terumi Nakajima +5 more
TL;DR: The results suggest that the linear amphipathic peptides in spider venoms and neuropeptides cooperate to capture insects efficiently.
References
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Magainins, a class of antimicrobial peptides from Xenopus skin: isolation, characterization of two active forms, and partial cDNA sequence of a precursor
TL;DR: 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.
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SOPMA: significant improvements in protein secondary structure prediction by consensus prediction from multiple alignments
TL;DR: Improvements brought about by predicting all the sequences of a set of aligned proteins belonging to the same family are reported by improving the success rate in the prediction of the secondary structure of proteins.
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Construction of improved Escherichia-Pseudomonas shuttle vectors derived from pUC18/19 and sequence of the region required for their replication in Pseudomonas aeruginosa
TL;DR: The nucleotide sequence of the 1.9-kb PstI fragment from pRO1614, that allows stable maintenance of pMB1 (ColE1)-based cloning vectors in Pseudomonas, was determined and encodes a putative origin of replication, a replication-controlling protein, and the C terminus of the Tn3 beta-lactamase-encoding gene.
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Molecular Basis for Membrane Selectivity of an Antimicrobial Peptide, Magainin 2
TL;DR: It is concluded that the absence of any acidic phospholipids on the outer monolayer and the abundant presence of cholesterol, combined with the lack of the transmembrane potential, contribute to the protection of erythrocytes from magainin's attack.