Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 561484
Title Selection of antimicrobial frog peptides and temporin-1DRa analogs for treatment of bacterial infections based on their cytotoxicity and differential activity against pathogens
Author(s) Gaiser, R.A.; Ayerra Mangado, J.; Mechkarska, M.; Kaman, W.E.; Baarlen, P. van; Conlon, J.M.; Wells, J.M.
Source Chemical Biology and Drug Design (2019). - ISSN 1747-0285 - 15 p.
DOI https://doi.org/10.1111/cbdd.13569
Department(s) WIAS
VLAG
Host-Microbe Interactomics
Publication type Refereed Article in a scientific journal
Publication year 2019
Keyword(s) Antimicrobial Peptide - Biological Screening
Abstract Cationic, amphipathic, α‐helical host‐defense peptides (HDPs) that are naturally secreted by certain species of frogs (Anura) possess potent broad‐spectrum antimicrobial activity and show therapeutic potential as alternatives to treat infections by multi‐drug resistant pathogens. Fourteen amphibian skin peptides and twelve analogues of temporin‐1DRa were studied for their antimicrobial activities against clinically relevant human or animal skin infection‐associated pathogens. For comparison, antimicrobial potencies of frog skin peptides against a range of probiotic lactobacilli were determined. We used the VITEK 2 system to define a profile of antibiotic susceptibility for the bacterial panel. The minimal inhibitory concentration (MIC) values of the naturally occurring temporin‐1DRa, CPF‐AM1, alyteserin‐1c, hymenochirin‐2B, and hymenochirin‐4B for pathogenic bacteria were 3‐ to 9‐fold lower than the values for the tested probiotic strains. Similarly, temporin‐1DRa and its [Lys4], [Lys5] and [Aib8] analogues showed 5‐ to 6.5‐fold greater potency against the pathogens. In the case of PGLa‐AM1, XT‐7, temporin‐1DRa and its [D‐Lys8] and [Aib13] analogues, no apoptosis or necrosis was detected in human peripheral blood mononuclear cells at concentrations below or above the MIC. Given the differential activity against commensal bacteria and pathogens, some of these peptides are promising candidates for further development into therapeutics for topical treatment of skin infections
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