Journal ArticleDOI
Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin
TLDR
Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested, and Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.Abstract:
A physiologically diverse range of Gram-positive and Gram-negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 micrograms/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na+, K+, Mg2+ or Ca2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.read more
Citations
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Journal ArticleDOI
Lactosmart: A Novel Therapeutic Molecule for Antimicrobial Defense.
Jiya Singh,Viswanathan Vijayan,Saiema Ahmedi,Pradeep Pant,Nikhat Manzoor,Tej P. Singh,Pradeep Sharma,Sujata Sharma +7 more
TL;DR: In this article, a 21-kDa basic fragment of Lactoferrin (LF) was digested by trypsin, and the resulting hydrolysates were studied with respect to their antimicrobial properties.
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Mammals' humoral immune proteins and peptides targeting the bacterial envelope: from natural protection to therapeutic applications against multidrug‐resistant Gram‐negatives
TL;DR: Bacterial envelope‐targeting proteins/peptides of the mammalian immune system that are most likely to have therapeutic applications are reviewed and weak points and knowledge gaps are identified and areas for future work to obtain successful envelope-targeting therapeutic options to tackle the challenge of antimicrobial resistance are suggested.
Journal ArticleDOI
Inhibitory Effects of Synthetic Peptides Containing Bovine Lactoferrin C-lobe Sequence on Bacterial Growth.
TL;DR: In this study, Asn-Leu-Asn-Arg was selected and chemically synthesized based on the partial sequences of bovine lactoferrin tryptic fragments to show antibacterial activity, and it is expected that this synthetic peptide would be the first peptide sequence from the bovines lact oferrin C-lobe that shows antib bacterial activity.
Book ChapterDOI
Whey Proteins and Their Value-Added Applications
R. Singh,Geetanjali +1 more
TL;DR: A comprehensive coverage of literature is discussed for the effective utilization of whey for the production of value-added products in this article, where the authors present a method based on bioorganic chemistry and biotechnological techniques.
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Identification and characterization of SaRpAMP, a 60S ribosomal protein L27-derived antimicrobial peptide from amur catfish, Silurus asotus.
TL;DR: The identified peptide, SaRpAMP, was the first antimicrobial peptide reported to be derived from the C-terminal region of 60S ribosomal protein L27, and it is suggested that the action mechanism involved the interaction of the peptide with the bacterial membranes.
References
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Journal ArticleDOI
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Wayne Robert Bellamy,Mitsunori Takase,Koji Yamauchi,Hiroyuki Wakabayashi,Kouzou Kawase,Mamoru Tomita +5 more
TL;DR: The studies suggest this domain is the structural region responsible for the bacterial properties of lactoferrin, having effectiveness against various Gram-negative and Gram-positive bacteria at concentrations between 0.3 microM and 3.0 microM, depending on the target strain.
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TL;DR: The D enantiomers of three naturally occurring antibiotics--cecropin A, magainin 2 amide, and melittin--were synthesized and it is suggested that the mode of action of these peptides on the membranes of bacteria, erythrocytes, plasmodia, and artificial lipid bilayers may be similar and involves the formation of ion-channel pores spanning the membranes, but without specific interaction with chiral receptors or enzymes.
Journal ArticleDOI
Cell-free immunity in insects.
Hans G. Boman,Dan Hultmark +1 more
TL;DR: The authors showed that at least two of the cecropins originate from a gene duplication and that the biosynthesis has been initiated on RNA and tissue levels on both RNA and DNA levels.
Journal ArticleDOI
Killing of gram-negative bacteria by lactoferrin and lysozyme.
rd R T Ellison,T. J. Giehl +1 more
TL;DR: Dialysis chamber studies indicate that bacterial killing requires direct contact with lactoferrin, and work with purified LPS suggests that this relates to direct LPS-binding by the protein, suggesting that their interaction contributes to host defense.
Journal ArticleDOI
A bactericidal effect for human lactoferrin
TL;DR: Streptococcus mutans and Vibrio cholerae, but not Escherichia coli, were killed by incubation with purified human apolact oferrin, contingent upon the metal-chelating properties of the lactoferrin molecule.