The antimicrobial activity of bovine lactoferrin is attributed to lactoferricin, situated in the N1-domain. Based on common features of antimicrobial peptides, a second putative antimicrobial domain was identified in the N1-domain of lactoferrin, designated lactoferrampin. This novel peptide exhibited candidacidal activity, which was substantially higher than the activity of lactoferrin. Furthermore, lactoferrampin was active against Bacillus subtilis, Escherichia coli, and Pseudomonas aeruginosa, but not against the fermenting bacteria Actinomyces naeslundii, Porphyromonas gingivalis, Streptococcus mutans and Streptococcus sanguis. Notably, lactoferrampin is located in the N1-domain in close proximity to lactoferricin, which plays a crucial role in membrane-mediated activities of lactoferrin.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.peptides.2003.12.006 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
A Review on cLF36, a Novel Recombinant Antimicrobial Peptide-Derived Camel Lactoferrin.
Probiotics Antimicrob Proteins
October 2024
Department of Avian Diseases, Faculty of Veterinary Medicine, University of Tehran, Tehran, Iran.
Lactoferrin is an antimicrobial peptide (AMP) playing a pivotal role in numerous biological processes. The primary antimicrobial efficacy of lactoferrin is associated with its N-terminal end, which contains various peptides, such as lactoferricin and lactoferrampin. In this context, our research team has developed a refined chimeric 42-mer peptide known as cLF36 over the past few years.
View Article and Find Full Text PDFMicroencapsulated Encoding Lactoferricin-Lactoferrampin Targeted Intestine against Infection.
Nutrients
December 2023
College of Veterinary Medicine, Northeast Agricultural University, Harbin 150030, China.
serovar Typhimurium () is an important foodborne pathogen that infects both humans and animals and develops acute gastroenteritis. As porcine intestines are relatively similar to the human ones due to their relatively similar sizes and structural similarity, causes analogous symptoms in both. Novel strategies for controlling infection are also desired, such as mucosal-targeted delivery of probiotics and antimicrobial peptides.
View Article and Find Full Text PDFEffects of Lactococcus lactis MG1363 producing fusion proteins of bovine lactoferricin-lactoferrampin on growth, intestinal morphology and immune function in weaned piglet.
J Appl Microbiol
September 2019
College of Veterinary Medicine, Northeast Agricultural University, Harbin, China.
Aims: We developed a strategy for localized delivery of the LFCA (lactoferricinlactoferrampin), which is actively synthesized in situ by Lactococcus lactis (pAMJ399-LFCA/LLMG1363), and explored the possibility of using pAMJ399-LFCA/LLMG1363 as an alternative additive diet to antibiotics.
Methods And Results: The antimicrobial activities of the LFCA derived from pAMJ399-LFCA/LLMG1363 were tested in vitro. The results showed that LFCA had an inhibitory effect on Staphylococcus aureus, Escherichia coli and Salmonella enteritidis.
Antimicrobial Activity of Lactoferrin-Related Peptides and Applications in Human and Veterinary Medicine.
Molecules
June 2016
Department of Drug Science and Technology, University of Torino, Torino 10125, Italy.
Antimicrobial peptides (AMPs) represent a vast array of molecules produced by virtually all living organisms as natural barriers against infection. Among AMP sources, an interesting class regards the food-derived bioactive agents. The whey protein lactoferrin (Lf) is an iron-binding glycoprotein that plays a significant role in the innate immune system, and is considered as an important host defense molecule.
View Article and Find Full Text PDFSequence context induced antimicrobial activity: insight into lipopolysaccharide permeabilization.
Mol Biosyst
June 2014
Biomolecular NMR and Drug Design Laboratory, Department of Biophysics, Bose Institute, P-1/12 CIT Scheme VII (M), Kolkata 700054, India.
Lactoferrampin (WR17, Trp 268-Arg 284), an antimicrobial peptide, is known to have significant antibacterial and candidacidal activities. However, there are no previous studies explaining how WR17 permeabilizes the outer membrane of Gram negative bacteria and neutralizes endotoxins. In this study we used a series of assays like antimicrobial activity, calcein leakage, NPN dye uptake and endotoxin neutralization assay to show that the sequence context of WR17 modulates its multi-faceted activities.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!