ArticleWorld journal of microbiology & biotechnology2017
Effects of lactoferrin derived peptides on simulants of biological warfare agents.
Article in World journal of microbiology & biotechnology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 20 citations in OpenAlex.
- Synergistic Antimicrobial Action of Lactoferrin-Derived Peptides and Quorum Quenching Enzymes.International journal of molecular sciences · 2023Article
- Investigating the Specificity of the Dehydration and Cyclization Reactions in Engineered Lanthipeptides by Synechococcal SyncM.ACS synthetic biology · 2023Article
- Bioactive Antimicrobial Peptides: A New Weapon to Counteract Zoonosis.Microorganisms · 2022Review
- Antimicrobial effect and mechanism of bovine lactoferrin against the potato common scab pathogen Streptomyces scabiei.PloS one · 2022Article
- Lactoferrin: A Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes.Molecules (Basel, Switzerland) · 2021Review
- Exploiting Lactoferricin (17-30) as a Potential Antimicrobial and Antibiofilm Candidate Against Multi-Drug-Resistant EnteroaggregativeFrontiers in microbiology · 2020Article
- Expression and Purification of the Main Component Contained in Camel Milk and Its Antimicrobial Activities Against Bacterial Plant Pathogens.Probiotics and antimicrobial proteins · 2018Article
- LFchimera protects HeLa cells from invasion by Yersinia spp. in vitro.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2018Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactoferrin (LF) is an important immune protein in neutrophils and secretory fluids of mammals. Bovine LF (bLF) harbours two antimicrobial stretches, lactoferricin and lactoferampin, situated in close proximity in the N1 domain. To mimic these antimicrobial domain parts a chimeric peptide (LFchimera) has been constructed comprising parts of both stretches (LFcin17-30 and LFampin265-284). To investigate the potency of this construct to combat a set of Gram positive and Gram negative bacteria which are regarded as simulants for biological warfare agents, the effect on bacterial killing, membrane permeability and membrane polarity were determined in comparison to the constituent peptides and the native bLF. Furthermore we aimed to increase the antimicrobial potency of the bLF derived peptides by cationic amino acid substitutions. Overall, the bactericidal activity of the peptides could be related to membrane disturbing effects, i.e. membrane permeabilization and depolarization. Those effects were most prominent for the LFchimera. Arginine residues were found to be crucial for displaying antimicrobial activity, as lysine to arginine substitutions resulted in an increased antimicrobial activity, affecting mostly LFampin265-284 whereas arginine to lysine substitutions resulted in a decreased bactericidal activity, predominantly in case of LFcin17-30.
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