Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity

Rekdal, Øystein; Andersen, Jill; Vorland, Lars H.; Svendsen, John S.

doi:10.1002/(sici)1099-1387(199901)5:1<32::aid-psc172>3.0.co;2-9

Cited by 69 publications

(57 citation statements)

References 48 publications

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“…A QSAR study on bovine LFcin (LF f(14-41)) analogs (8 peptides with 12-19 amino acid residues) was conducted to study antimicrobial activity against Escherichia coli and Staphylococcus aureus. 71 Large and negatively charged peptides or peptides with a high hydrophobic moment (m) displayed high antimicrobial activity against E. coli and S. aureus, respectively. In another study, 19 murine LFcin (LF f(16-30)) analog peptides were used to build a QSAR model in relation to their antimicrobial activity against E. coli and S. aureus.…”

Section: Antimicrobial Peptidesmentioning

confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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Section: Antimicrobial Peptidesmentioning

confidence: 99%

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Nongonierma

Fitzgerald

2016

RSC Adv.

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“…Most of the resulting peptides Zhao et al 2111 by the incorporation of one ore more additional Trp displayed a substantial increase in the antimicrobial activity. LfcinB15 generated by replacing the residue Met 10 with Trp showed improved activity (Rekdal et al, 1999;Strøm et al, 2002). In the present study, a novel AMP LFM23 was designed according to LfcinB and melittin.…”

Section: Discussionmentioning

confidence: 95%

“…Numerous studies have been carried out on the structure-activity relation of LfcinB and its derivatives. Rekdal et al (1999) and Strøm et al (2000) synthesized a derivative LfcinB15 consisting of residues 1 to 15 of LfcinB. It has only minor loss of antimicrobial activity relative to the native peptide LfcinB.…”

Section: Discussionmentioning

confidence: 99%

Design, synthesis and antibacterial activity of a novel hybrid antimicrobial peptide LFM23

Zhao¹,

DeShui²,

Gong³

et al. 2012

Afr. J. Biotechnol.

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Antimicrobial peptides produced by many tissues and cell types of invertebrates, insects and humans as part of their innate immune system, have received increasing attention as potential candidates due to their administration as pharmaceutical agents. In the present study, a novel hybrid antimicrobial peptide LFM23 consisting of 23 amino acid residues was designed based on the primary sequences of bovine lactoferricin (LfcinB) and melittin. The peptide was synthesized by chemical method of solidphase synthesis with a purity of more than 98% after reverse phase high performance liquid chromatography. Antimicrobial activity assay showed that LFM23 had strong antibacterial abilities, and the minimum inhibitory concentrations against Escherichia coli AT CC25922, Salmonella typhimurium ATCC12291, Pseudomonas aeruginosa ATCC27853, Staphylococcus aureus ATCC25923, Pichia pastoris GS115, were 32, 32, 64, 32 and 256 μg/ml, respectively. The hemolytic assays indicated that LFM23 had no hemolytic action in vitro at antimicrobial concentration. The results demonstrate that the peptide LFM23 has a good application prospect as clinically useful antimicrobial agents.

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“…There has been a significant amount of work aimed at pinpointing the exact amino acid residues required for the bioactivity of lactoferricin [11]. Two tryptophan residues at positions 6 and 8 have been found to be necessary for antimicrobial activity [17].…”

Section: Discussionmentioning

confidence: 99%

“…The incubation of lactoferricin with LB11 cells, however, resulted in a number of peaks corresponding to almost thorough cleavage at every amino acid residue in the sequence. Masses corresponding to proteolysis at residues 1, 2, 3, 5, 6, 7, 10, 11,12,13,14,15,17,22, and 24 were observed, suggesting random enzymatic digestion. In contrast, products of lactoferricin incubated with cells of strain LB20 mostly showed cleavage at the anticipated locations, near arginine 4, 5, 9, and 23 and lysine 2 and 11.…”

Section: Mass Spectrometric Analysis Of Lb-lactoferricin Degradation mentioning

confidence: 99%

Hydrolytic breakdown of lactoferricin by lactic acid bacteria

Paul

Somkuti

2009

J Ind Microbiol Biotechnol

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Lactoferricin is a 25-amino acid antimicrobial peptide fragment that is liberated by pepsin digestion of lactoferrin present in bovine milk. Along with its antibacterial properties, lactoferricin has also been reported to have immunostimulatory, antiviral, and anticarcinogenic effects. These attributes provide lactoferricin and other natural bioactive peptides with the potential to be functional food ingredients that can be used by the food industry in a variety of applications. At present, commercial uses of these types of compounds are limited by the scarcity of information on their ability to survive food processing environments. We have monitored the degradation of lactoferricin during its incubation with two types of lactic acid bacteria used in the yogurt-making industry, Streptococcus thermophilus and Lactobacillus delbrueckii ssp. bulgaricus, with the aim of assessing the stability of this milk protein-derived peptide under simulated yogurt-making conditions. Analysis of the hydrolysis products isolated from these experiments indicates degradation of this peptide near neutral pH by lactic acid bacteria-associated peptidases, the extent of which was influenced by the bacterial strain used. However, the data also showed that compared to other milk-derived bioactive peptides that undergo complete degradation under these conditions, the 25-amino acid lactoferricin is apparently more resistant, with approximately 50% of the starting material remaining after 4 h of incubation. These findings imply that lactoferricin, as a natural milk protein-derived peptide, has potential applications in the commercial production of yogurt-like fermented dairy products as a multi-functional food ingredient.

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Construction and synthesis of lactoferricin derivatives with enhanced antibacterial activity

Cited by 69 publications

References 48 publications

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Learnings from quantitative structure–activity relationship (QSAR) studies with respect to food protein-derived bioactive peptides: a review

Design, synthesis and antibacterial activity of a novel hybrid antimicrobial peptide LFM23

Hydrolytic breakdown of lactoferricin by lactic acid bacteria

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