Antimicrobial peptides from skin secretions of Rana esculenta. Molecular cloning of cDNAs encoding esculentin and brevinins and isolation of new active peptides.
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TLDR
Ten new peptides, ranging in size from 24 to 46 residues, all possessing an intramolecular disulfide bridge located at the carboxyl-terminal end, were isolated from skin secretions of R. esculenta and it is demonstrated that esculentin-1 also inhibits the growth of Pseudomonas aeruginosa, Candida albicans, and Saccharomyces cerevisiae.About:
This article is published in Journal of Biological Chemistry.The article was published on 1994-04-22 and is currently open access. It has received 227 citations till now. The article focuses on the topics: Antimicrobial peptides & Temporin.read more
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Peptide antibiotics and their role in innate immunity.
TL;DR: The results obtained imply that the polypeptide-like structure dominates in the structure derived from Polypeptides with S-S Bonds while in the case of Peptides Giving Mainly or Only fJ-Sheet Structures, the polymethine-rich structure is preferred.
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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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Antimicrobial peptides in insects; structure and function
TL;DR: This review presents the main results obtained during the last four years in the field of antimicrobial peptides from insects with a special focus on the proline-rich and cysteine-rich peptides.
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Antimicrobial peptides: premises and promises.
TL;DR: Peptides, namely magainin and nisin have been shown to demonstrate contraceptive properties in vitro and in vivo and a few peptides have already entered clinical trials for the treatment of impetigo, diabetic foot ulcers and gastric helicobacter infections.
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Animal antimicrobial peptides: an overview.
David Andreu,Luis Rivas +1 more
TL;DR: This review provides a general introduction to the subject of antimicrobial peptides, with emphasis on aspects such as structural types, post-translational modifications, mode of action or mechanisms of resistance.
References
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TL;DR: Three computer programs for comparisons of protein and DNA sequences can be used to search sequence data bases, evaluate similarity scores, and identify periodic structures based on local sequence similarity.
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Rapid production of full-length cDNAs from rare transcripts: amplification using a single gene-specific oligonucleotide primer
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Cloning in single-stranded bacteriophage as an aid to rapid DNA sequencing
TL;DR: An approach to DNA sequencing using chain-terminating inhibitors (Sanger et al., 1977) combined with cloning of small fragments of DNA in a single-stranded DNA bacteriophage is described, determining the 2771-nucleotide sequence of the largest MboI restriction enzyme fragment from human mitochondrial DNA.
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Patterns of Amino Acids near Signal‐Sequence Cleavage Sites
TL;DR: In this paper, some such patterns, based on a sample of 78 eukaryotic signal sequences, are presented and discussed, and a first attempt at formulating rules for the prediction of cleavage sites is made.
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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.