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1.
Inhibition of iron/ascorbate-induced lipid peroxidation by an N-terminal peptide of bovine lactoferrin and its acylated derivatives. 总被引:3,自引:0,他引:3
H Wakabayashi H Matsumoto K Hashimoto S Teraguchi M Takase H Hayasawa 《Bioscience, biotechnology, and biochemistry》1999,63(5):955-957
Bovine lactoferrin (LF) and lactoferricin B (LFcin B), an antimicrobial peptide derived from bovine LF, inhibited thiobarbituric acid-reactive substance (TBARS) formation in a iron/ascorbate-induced liposomal phospholipid peroxidation system. The inhibition of TBARS formation occurred with N-acylated 9-mer peptides with a core sequence of LFcin B and, compared to LFcin B, their antioxidant effect was clearly observed at a concentration almost 100 times lower. 相似文献
2.
G. Xu W. Xiong Q. Hu P. Zuo B. Shao F. Lan X. Lu Y. Xu S. Xiong 《Journal of applied microbiology》2010,109(4):1311-1318
Aims: To investigate the bactericidal activity of lactoferrin‐derived peptides and a new LF‐derived peptides chimera (LFchimera) against P. aeruginosa and the influence on virulence factors of P. aeruginosa. Methods and Results: Lactoferricin (LFcin) and lactoferrampin (LFampin) are highly bioactive peptides isolated from the N‐terminal region of lactoferrin (LF) by pepsin digestion. In this study, we designed LFchimera containing LFcin amino acids 17‐30 and LFampin amino acids 268‐284. Pseudomonas aeruginosa cells were incubated in medium with peptides at different concentrations, and then the assays of viability, pyocyanin, elastase activity and biofilm formation of P. aeruginosa were performed. We found that the concentration‐dependent antibactericidal activity and down‐regulating pyocyanin, elastase and biofilm formation of LFchimera were significantly stronger than those of LF, LFcin, LFampin or LFcin plus LFampin. Conclusions: Our results indicated that LF, LFcin, LFampin and LFchimera were potential candidates to combat P. aeruginosa, and LFchimera was the most effective in them. Significance and Impact of the Study: The new LFchimera has better activity against P. aeruginosa than LF, LFcin and LFampin and may be a promising new compound for treatment of P. aeruginosa infection. 相似文献
3.
Wakabayashi H Kuwata H Yamauchi K Teraguchi S Tamura Y 《Bioscience, biotechnology, and biochemistry》2004,68(4):853-860
We investigated the transfer of dietary bovine lactoferrin (LF) and its functional lactoferricin (LFcin) B-containing fragments to the portal blood of healthy adult rats by using several techniques. After a single administration of (125)I-labeled LF, radioactive bands were detected in autoradioluminograms of the portal blood, but similar bands were also observed after the administration of [(125)I]NaI. Although ovalbumin was detected by ELISA at 3-18 ng/ml in the portal blood plasma after an overnight administration, no LF was detected (< or =1.5 ng/ml). The antibody-captured ovalbumin fragments, but not the LF fragments, were detected in the plasma by surface-enhanced laser desorption/ionization affinity mass spectrometry (SELDI affinity MS). We finally attempted to detect the LFcin B-containing fragments by SELDI affinity MS with on-chip LFcin B-conversion, but could not detect them (< or =1 ng/ml) in the portal blood after the LF ingestion. The level of LF or its functional fragments transferred to the portal blood was therefore extremely low, if any. 相似文献
4.
Escherichia coli (E. coli) are the most common aerobic gram-negative bacilli in a normal intestinal tract. They cause most of the intra-abdominal infections,
wound infections associated with abdominal surgery, and septicemia. Most of these infections are of endogenous intestinal
origin. Lactoferrin (LF) is an iron-binding glycoprotein found in milk and various external secretions. This protein has been
found to have a number of biological functions, including antimicrobial, anti-cancer, antioxidant, and immunomodulatory effects.
Partial degradation of LF by pepsin can give rise to peptides termed lactoferricin (LFcin) with more potent antimicrobial
activity. LF and LFcin have been shown to inhibit the growth of a number of pathogenic bacteria (including E. coli and antibiotic-resistant strains), fungi, and even viruses in both in vitro and in vivo studies. We previously demonstrated
that both recombinant porcine LF (pLF) produced from yeast and a synthetic 20-residue porcine LFcin peptide exhibit antimicrobial
activity in vitro. In one of our recent studies, we performed pathogen challenges, including pathogenic E. coli, Staphylococcus aureus and Candida albicans, of the digestive tract of a transgenic milk-fed animal model. The results showed that LF has broad spectrum antimicrobial
activity in the digestive tract and protects the mucosa of the small intestine from injury. Our following study also revealed
that pLF as a feedstuff additive enhances avian immunity, including antibody formation and cell-mediated immunity. All of
these results suggest that LF could be a novel natural protein in the treatment and prevention of infections with E. coli or antibiotic-resistant bacteria strains. 相似文献
5.
Mauricio Arias Lindsey J. McDonald Evan F. Haney Kamran Nazmi Jan G. M. Bolscher Hans J. Vogel 《Biometals》2014,27(5):935-948
Lactoferrin (LF) is an important antimicrobial and immune regulatory protein present in neutrophils and most exocrine secretions of mammals. The antimicrobial activity of LF has been related to the presence of an antimicrobial peptide sequence, called lactoferricin (LFcin), located in the N-terminal region of the protein. The antimicrobial activity of bovine LFcin is considerably stronger than the human version. In this work, chimera peptides combining segments of bovine and human LFcin were generated in order to study their antimicrobial activity and mechanism of action. In addition, the relevance of the conserved disulfide bridge and the resulting cyclic structure of both LFcins were analyzed by using “click chemistry” and sortase A-catalyzed cyclization of the peptides. The N-terminal region of bovine LFcin (residues 17–25 of bovine LF) proved to be very important for the antimicrobial activity of the chimera peptides against E. coli, when combined with the C-terminal region of human LFcin. Similarly the cyclic bovine LFcin analogs generated by “click chemistry” and sortase A preserved the antimicrobial activity of the original peptide, showing the significance of these two techniques in the design of cyclic antimicrobial peptides. The mechanism of action of bovine LFcin and its active derived peptides was strongly correlated with membrane leakage in E. coli and up to some extent with the ability to induce vesicle aggregation. This mechanism was also preserved under conditions of high ionic strength (150 mM NaCl) illustrating the importance of these peptides in a more physiologically relevant system. 相似文献
6.
Héctor Flores-Villase?or Adrian Canizalez-Román Magda Reyes-Lopez Kamram Nazmi Mireya de la Garza Jorge Zazueta-Beltrán Nidia León-Sicairos Jan G. M. Bolscher 《Biometals》2010,23(3):569-578
Increased prevalence of antibiotic-resistant bacteria has become a major threat to the health sector worldwide due to their
virulence, limited therapeutic options and distribution in both hospital and community settings. Discovery and development
of new agents to combat antibiotic-resistant bacteria is thus needed. This study therefore aimed to evaluate the ability of
bovine lactoferrin (LF), peptides from two antimicrobial domains lactoferricin B (LFcin17-30) and lactoferrampin (LFampin265-284)
and a chimeric construct (LFchimera) containing both peptides, as potential bactericidal agents against clinical isolates
of antibiotic-resistant Staphylococcus aureus and Escherichia coli. Results in kinetics of growth show that LF chimera and peptides inhibited the growth of both bacterial species. By confocal
microscopy and flow cytometry it was observed that LF and FITC-labeled peptides are able to interact with these bacteria and
cause membrane permeabilization, as monitored by propidium iodide staining, these effects were decreased by preincubation
with lipopolysaccharide in E. coli. By electron microscopy, a clear cellular damage was observed in bacteria after treatments with LFchimera and peptides, suggesting
that interaction and membrane disruption are probably involved as a mechanism of action. In conclusion, results show that
LFchimera, LF and peptides have potential as bactericidal agents in the antibiotic-resistant strains of S.
aureus and E. coli and also the work strongly suggest that LFcin17-30 and LFampin265-284 acts synergistically with antibiotics against multidrug
resistant EPEC and MRSA in vitro. 相似文献
7.
Increased Staphylococcus-killing activity of an antimicrobial peptide,lactoferricin B,with minocycline and monoacylglycerol 总被引:1,自引:0,他引:1
Wakabayashi H Teraguchi S Tamura Y 《Bioscience, biotechnology, and biochemistry》2002,66(10):2161-2167
This study aimed to find antibiotics or other compounds that could increase the antimicrobial activity of an antimicrobial peptide, lactoferricin B (LFcin B), against Staphylococcus aureus, including antibiotic-resistant strains. Among conventional antibiotics, minocycline increased the bactericidal activity of LFcin B against S. aureus, but methicillin, ceftizoxime, and sulfamethoxazole-trimethoprim did not have such an effect. The combination of minocycline and LFcin B had synergistic effects against three antibiotic-resistant strains of S. aureus, according to result of checkerboard analysis. Screening of 33 compounds, including acids and salts, alcohols, amino acids, proteins and peptides, sugar, and lipids, showed that medium-chain monoacylglycerols increased the bactericidal activity of LFcin B against three S. aureus strains. The short-term killing test in water and the killing curve test in growing cultures showed that a combination of LFcin B and monolaurin (a monoacylglycerol with a 12-carbon acyl chain) killed S. aureus more rapidly than either agent alone. These findings may be helpful in the application of antimicrobial peptides in medical or other situations. 相似文献
8.
van der Kraan MI van Marle J Nazmi K Groenink J van 't Hof W Veerman EC Bolscher JG Nieuw Amerongen AV 《Peptides》2005,26(9):1537-1542
Antimicrobial peptides allegedly exert their action on microbial membranes. Bovine lactoferrin enfold two antimicrobial domains, lactoferricin B (LFcin B) and lactoferrampin (LFampin). Effects of representative peptides thereof on the membranes of Candida albicans and Escherichia coli were investigated. Confocal laser scanning microscopy revealed that these peptides were internalized within a few minutes, concurrently with disrupting membrane integrity as indicated by freeze-fracture transmission electron microscopy. The most striking findings were induction of distinct vesicle-like structures in the membrane of C. albicans by the LFampin peptide, and detachment of the outer membrane and surface protrusions in E. coli by the LFcin B peptide. 相似文献
9.
Positive selection drives lactoferrin evolution in mammals 总被引:1,自引:0,他引:1
Lactoferrin (LF) is a member of the transferrin family that is abundantly expressed and secreted by glandular epithelial cells.
The biological functions of LF involve in iron homeostasis regulation of the body and antibacterial activity. Previous studies
demonstrated that it had a high cationic N-terminal domain that could interact with glycosaminoglycans, lipopolysaccharides
and the bacterial virulence protein. Two anti-microbial peptides, lactoferricin (LFcin) and lactoferrampin (LFampin), were
also isolated and identified in N-terminal of LF. Although the antibacterial mechanism was carefully studied, little was known
about the molecular evolution of LF. In this study, we estimated the nonsynonymous-to-synonymous substitution ratios (
w = dN \mathord