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Keywords = microbicidy

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18 pages, 4442 KB  
Article
A Bacterial Myeloperoxidase with Antimicrobial Properties
by Claire Céré, Brigitte Delord, Parfait Kenfack Ymbe, Léa Vimbert, Jean-Paul Chapel and Claire Stines-Chaumeil
BioTech 2023, 12(2), 33; https://doi.org/10.3390/biotech12020033 - 5 May 2023
Cited by 5 | Viewed by 3842
Abstract
The four mammalian peroxidases (myeloperoxidase, eosinophilperoxidase, lactoperoxidase, and thyroid peroxidase) are widely studied in the literature. They catalyze the formation of antimicrobial compounds and participate in innate immunity. Owing to their properties, they are used in many biomedical, biotechnological, and agro-food applications. We [...] Read more.
The four mammalian peroxidases (myeloperoxidase, eosinophilperoxidase, lactoperoxidase, and thyroid peroxidase) are widely studied in the literature. They catalyze the formation of antimicrobial compounds and participate in innate immunity. Owing to their properties, they are used in many biomedical, biotechnological, and agro-food applications. We decided to look for an enzyme that is easiest to produce and much more stable at 37 °C than mammalian peroxidases. To address this question, a peroxidase from Rhodopirellula baltica, identified by bioinformatics tools, was fully characterized in this study. In particular, a production and purification protocol including the study of heme reconstitution was developed. Several activity tests were also performed to validate the hypothesis that this peroxidase is a new homolog of mammalian myeloperoxidase. It has the same substrate specificities as the human one and accepts I, SCN, Br, and Cl as (pseudo-) halides. It also exhibits other auxiliary activities such as catalase and classical peroxidase activities, and it is very stable at 37 °C. Finally, this bacterial myeloperoxidase can kill the Escherichia coli strain ATCC25922, which is usually used to perform antibiograms. Full article
(This article belongs to the Section Medical Biotechnology)
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15 pages, 1239 KB  
Review
Cyclic Peptides as Novel Therapeutic Microbicides: Engineering of Human Defensin Mimetics
by Annarita Falanga, Ersilia Nigro, Margherita Gabriella De Biasi, Aurora Daniele, Giancarlo Morelli, Stefania Galdiero and Olga Scudiero
Molecules 2017, 22(7), 1217; https://doi.org/10.3390/molecules22071217 - 20 Jul 2017
Cited by 84 | Viewed by 10725
Abstract
Cyclic peptides are receiving significant attention thanks to their antimicrobial activity and high serum stability, which is useful to develop and design novel antimicrobial agents. Antimicrobial peptides appear to be key components of innate defences against bacteria, viruses, and fungi. Among the others, [...] Read more.
Cyclic peptides are receiving significant attention thanks to their antimicrobial activity and high serum stability, which is useful to develop and design novel antimicrobial agents. Antimicrobial peptides appear to be key components of innate defences against bacteria, viruses, and fungi. Among the others, defensins possess a strong microbicidial activity. Defensins are cationic and amphipathic peptides with six cysteine residues connected by three disulfide bonds found in plants, insects, and mammals; they are divided in three families: α-, β-, and θ-defensins. α-Defensins are contained in the primary granules of human neutrophils; β-defensins are expressed in human epithelia; and θ-defensins are pseudo-cyclic defensins not found in humans, but in rhesus macaques. The structural diversities among the three families are reflected in a different antimicrobial action as well as in serum stability. The engineering of these peptides is an exciting opportunity to obtain more functional antimicrobial molecules highlighting their potential as therapeutic agents. The present review reports the most recent advances in the field of cyclic peptides with a specific regard to defensin analogs. Full article
(This article belongs to the Special Issue Peptide-Based Drugs and Drug Delivery Systems)
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