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Journal ArticleDOI

Antimicrobial peptides isolated from skin secretions of the diploid frog, Xenopus tropicalis (Pipidae).

TLDR
Seven peptides with antimicrobial activity were isolated from norepinephrine-stimulated skin secretions of the diploid clawed frog, Xenopus tropicalis, suggesting that the species are not closely related phylogenetically.
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This article is published in Biochimica et Biophysica Acta.The article was published on 2001-11-26. It has received 84 citations till now. The article focuses on the topics: Antimicrobial peptides & Peptide sequence.

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Citations
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Journal ArticleDOI

Antifungal activity of epithelial secretions from selected frog species of South Africa

TL;DR: From this study it appears that bioprospecting of South African frog species has the potential to yield potential therapeutic lead agents.
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Host-defense and trefoil factor family peptides in skin secretions of the Mawa clawed frog Xenopus boumbaensis (Pipidae).

TL;DR: The primary structures of the peptides suggest a close phylogenetic relationship between X. boumbaensis and the octoploid frogs Xenopus amieti and Xenopus andrei and it is suggested that they diverged from a common ancestor by allopatric speciation.
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Peptidomic analysis of the extensive array of host-defense peptides in skin secretions of the dodecaploid frog Xenopus ruwenzoriensis (Pipidae)

TL;DR: Cl cladistic analyses based upon the primary structures of the host-defense peptides provide support for an evolutionary scenario in which X. ruwenzoriensis arose from an allopolyploidization event involving an octoploid ancestor of the present-day frogs belonging to the Xenopus amieti species group and a tetraploid ancestorof Xenopus pygmaeus.
Journal ArticleDOI

The biological role of charge distribution in linear antimicrobial peptides

TL;DR: In this article , the authors focus on linear peptides, particularly those that are alpha-helical structured, and examine how their charge distribution and hydrophobic amino acids could modulate their biological activity.
References
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Journal ArticleDOI

Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins.

TL;DR: The algorithm is shown to be at least as good as, and usually superior to, the reported prediction methods assessed in the same way and the implication in protein folding is discussed.
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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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Cationic peptides: a new source of antibiotics

TL;DR: Antimicrobial cationic peptides are an important component of the innate defenses of all species of life as discussed by the authors, and different peptides may have antibacterial, anti-endotoxic, antibiotic-potentiating or antifungal properties.
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Amphipathic, α‐helical antimicrobial peptides

TL;DR: This review considers alpha-helical, antimicrobial peptides from the point of view of six interrelated structural and physicochemical parameters that modulate their activity and specificity: sequence, size, structuring, charge, amphipathicity, and hydrophobicity.
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Mode of action of linear amphipathic α-helical antimicrobial peptides

TL;DR: This review, which is focused on magainins, cecropins, and dermaseptins as representatives of the amphipathic alpha-helical antimicrobial peptides, supports the carpet-like rather the barrel-stave mechanism.
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