Lactoferricin

Gifford, Jessica L.; Hunter, Howard N.; Vogel, Hans J.

doi:10.1007/s00018-005-5373-z

Cited by 447 publications

(202 citation statements)

References 67 publications

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“…Furthermore, it will be interesting to compare analogous peptides derived from lactoferrin of different species. In the past, the antimicrobial characteristics of bovine lactoferrin-derived peptides have been compared in detail with those of their human counterparts (13). Because of its human origin, the hLF peptide is expected to be non-immunogenic.…”

Section: Discussionmentioning

confidence: 99%

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A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

Duchardt

Ruttekolk

Verdurmen

et al. 2009

Journal of Biological Chemistry

112

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The molecular events that contribute to the cellular uptake of cell-penetrating peptides (CPP) are still a matter of intense research. Here, we report on the identification and characterization of a 22-amino acid CPP derived from the human milk protein, lactoferrin. The peptide exhibits a conformation-dependent uptake efficiency that is correlated with efficient binding to heparan sulfate and lipid-induced conformational changes. The peptide contains a disulfide bridge formed by terminal cysteine residues. At concentrations exceeding 10 M, this peptide undergoes the same rapid entry into the cytoplasm that was described previously for the arginine-rich CPPs nona-arginine and Tat. Cytoplasmic entry strictly depends on the presence of the disulfide bridge. To better understand this conformation dependence, NMR spectroscopy was performed for the free peptide, and CD measurements were performed for free and lipidbound peptide. In solution, the peptides showed only slight differences in secondary structure, with a predominantly disordered structure both in the presence and absence of the disulfide bridge. In contrast, in complex with large unilamellar vesicles, the conformation of the oxidized and reduced forms of the peptide clearly differed. Moreover, surface plasmon resonance experiments showed that the oxidized form binds to heparan sulfate with a considerably higher affinity than the reduced form. Consistently, membrane binding and cellular uptake of the peptide were reduced when heparan sulfate chains were removed.

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Section: Discussionmentioning

confidence: 99%

“…The hLF N-terminal domain in particular carries potent activity against pathogens (13). In the gastrointestinal tract this domain can be cleaved through pepsin digestion resulting in the release of an antimicrobial peptide called lactoferricin (14).…”

mentioning

confidence: 99%

A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

Duchardt

Ruttekolk

Verdurmen

et al. 2009

Journal of Biological Chemistry

112

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“…The cationic domain of the N-terminal region of LF, lactoferricin, plays an important role in the direct bactericidal effects. 33,[36][37][38] Yoshinari et al reported that the modification of Ti surface with titaniumbinding peptides (minTBP-1) and lactoferricin showed a reduction in the bioactivity of P. gingivalis. 39 Although the antibacterial mechanism of LF on gram-positive pathogens is still not well understood, the interaction between LF and the cell membrane of gram-positive bacteria has been reported.…”

Section: B Inhibition Of S Gordonii Adhesion and The Bactericidal Ementioning

confidence: 99%

Inhibition of initial bacterial adhesion on titanium surfaces by lactoferrin coating

et al. 2014

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Because dental implant abutments are located at transmucosal sites, their surface should inhibit bacterial accumulation to prevent peri-implantitis. The authors examined the effects of human lactoferrin (LF), an antibacterial protein present in saliva, as an antibacterial coating on the titanium surface and evaluated its effects before and after mucin-containing artificial saliva (AS) incubation. In the control group, titanium disks were soaked in distilled water, whereas in the LF group, titanium disks were soaked in LF solution to coat the disks. In the control-AS and LF-AS groups, half of the control and LF disks were incubated with AS. To confirm LF adsorption, the fluorescence intensity of fluorescein isothiocyanate-labeled LF was measured. The LF and LF-AS groups showed significantly higher intensity than the control and control-AS groups (P < 0.01). There was no significant difference between the LF and LF-AS groups (P > 0.05). The amount of adhered Streptococcus gordonii significantly increased by incubation with AS (P < 0.01) and significantly decreased by adsorption of LF (P < 0.01). There was no interaction between the two factors, LF adsorption and AS incubation (P = 0.561). These results suggest that the adsorbed LF inhibited bacterial adhesion following AS incubation. According to qualitative LIVE/DEAD analysis, viable bacteria appeared to be decreased in the presence of LF and SEM observation indicated that altered morphologies increased in LF and LF-AS groups. These results suggest that the adsorbed LF remained on the titanium surface after incubation with AS, and the remaining LF inhibited bacterial adhesion and exhibited bactericidal effects. Therefore, the adsorption of LF on the abutment material appears to be effective in preventing peri-implantitis.

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“…In general, AMPs are cationic, often amphipathic, which primarily kill bacteria by interacting and disrupting their cell membrane [10][11][12][13] . In a previous study, we introduced the 1-11 antimicrobial sequence of the human lactoferrin protein (hLf), the hLf1-11 peptide, as a potent AMP with capacity to reduce bacterial adhesion on titanium implants 8 .…”

Section: Introductionmentioning

confidence: 99%

Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization

et al. 2015

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Dental implant failure can be associated to infections which develop into periimplantitis. In order to reduce biofilm formation, several strategies focusing on the use of antimicrobial peptides (AMP) have been studied. To covalently immobilize these molecules onto metallic substrates several techniques have been developed, including silanization and polymer brush prepared by surface-initiated atom transfer radical polymerization (ATRP), with varied peptide binding yield and antibacterial performance. The aim of the present study was to compare the efficiency of these methods to immobilize the lactoferrin-derived hLf1-11 antibacterial peptide onto titanium, and evaluate their antibacterial activity in vitro.Smooth titanium samples were coated with hLf1-11 peptide under three different conditions: silanization with APTES, and polymer brush based coatings with two different silanes. Peptide presence was determined by X-ray photoelectron spectroscopy and the mechanical stability of the coatings was studied under ultrasonication. The LDH assays confirmed that HFFs viability and proliferation were no affected by the treatments. The in vitro antibacterial properties of the modified surfaces were tested with two oral strains (Streptococcus sanguinis and Lactobacillus salivarius) showing an outstanding reduction. A higher decrease in bacterial attachment was noticed when samples were modified by ATRP methods compared to silanization. This effect is likely due to the capacity to immobilize more peptide on the surfaces using polymer brushes and the non-fouling nature of polymer PDMA segment.3

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Lactoferricin

Cited by 447 publications

References 67 publications

A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

A Cell-penetrating Peptide Derived from Human Lactoferrin with Conformation-dependent Uptake Efficiency

Inhibition of initial bacterial adhesion on titanium surfaces by lactoferrin coating

Antibacterial Properties of hLf1–11 Peptide onto Titanium Surfaces: A Comparison Study Between Silanization and Surface Initiated Polymerization

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