Histatin and lactoferrin derived peptides: Antimicrobial properties and effects on mammalian cells

Stallmann, Hein P.; Faber, Chris; Bronckers, A.L.J.J.; Blieck-Hogervorst, J.M.A. de; Brouwer, Carlo P.J.M.; Amerongen, A. van Nieuw; Wuisman, P.

doi:10.1016/j.peptides.2005.05.014

Cited by 42 publications

(30 citation statements)

References 15 publications

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“…The hLF(1-11) peptide did not cause haemolysis in phosphate buffered solutions at concentration up to 2.000 µg/mL. This is coherent with the results from Stallman et al [70]. Results indicate that salt concentration can markedly influence the haemolysis, similar to what is reported for other peptides [71] (Figure 2).…”

Section: Discussionsupporting

confidence: 90%

Structure-Activity Relationship Study of Synthetic Variants Derived from the Highly Potent Human Antimicrobial Peptide hLF(1-11)

Brouwer

Roscini

Cardinali

et al. 2018

CJMI

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Section: Discussionsupporting

confidence: 90%

Structure-Activity Relationship Study of Synthetic Variants Derived from the Highly Potent Human Antimicrobial Peptide hLF(1-11)

Brouwer

Roscini

Cardinali

et al. 2018

CJMI

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“…The antimicrobially active region in lactoferricin also included the first cationic domain of human LF comprising amino acid residues 1-11. This short 11-amino-acid-long peptide and the recently reported peptide comprising residues 153-183 of the LF molecule also have been shown to express antimicrobial activities (11,26,30,32).…”

Section: Fig 3 Effects Of Various Ph Levels On the Microbicidal Actmentioning

confidence: 66%

“…The only significant enhancing effect that any substitution (one or several) had on the antimicrobial activity compared with the natural sequence (20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31), as analyzed in BHI dil , was obtained with Orn in position 24 against C. albicans (not shown).…”

Section: Resultsmentioning

confidence: 99%

Structure-Microbicidal Activity Relationship of Synthetic Fragments Derived from the Antibacterial α-Helix of Human Lactoferrin

Håversen

Kondori²,

Baltzer

et al. 2010

Antimicrob Agents Chemother

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There is a need for new microbicidal agents with therapeutic potential due to antibiotic resistance in bacteria and fungi. In this study, the structure-microbicidal activity relationship of amino acid residues 14 to 31 (sequence 14-31) from the N-terminal end, corresponding to the antibacterial ␣-helix of human lactoferrin (LF), was investigated by downsizing, alanine scanning, and substitution of amino acids. Microbicidal analysis (99% killing) was performed by a microplate assay using Escherichia coli, Staphylococcus aureus, and Candida albicans as test organisms. Starting from the N-terminal end, downsizing of peptide sequence 14-31 showed that the peptide sequence 19-31 (KCFQWQRNMRKVR, HL9) was the optimal length for antimicrobial activity. Furthermore, HL9 bound to lipid A/lipopolysaccharide, as shown by neutralizing endotoxic activity in a Limulus assay. Alanine scanning of peptide sequence 20-31 showed that Cys20, Trp23, Arg28, Lys29, or Arg31 was important for expressing full killing activity, particularly against C. albicans. Substituting the neutral hydrophilic amino acids Gln24 and Asn26 for Lys and Ala (HLopt2), respectively, enhanced microbicidal activity significantly against all test organisms compared to the amino acids natural counterpart, also, in comparison with HL9, HLopt2 had more than 10-fold-stronger fungicidal activity. Furthermore, HLopt2 was less affected by metallic salts than HL9. The microbicidal activity of HLopt2 was slightly reduced only at pH 7.0, as tested in the pH range of 4.5 to 7.5. The results showed that the microbicidal activity of synthetic peptide sequences, based on the antimicrobial ␣-helix region of LF, can be significantly enhanced by optimizing the length and substitution of neutral amino acids at specific positions, thus suggesting a sequence lead with therapeutic potential.

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“…Dhvar5 presented a promising MIC of 0.5 mg/ml against a methicillin-resistant S. aureus (MRSA) that is lower than the reported elsewhere [8,9,12,29,30]. However, direct comparison of such values is very difficult, as a result of the lack of universal standardized methods to assess AMP activity, besides the use of different S. aureus strains.…”

Section: Discussionmentioning

confidence: 96%

Dhvar5 antimicrobial peptide (AMP) chemoselective covalent immobilization results on higher antiadherence effect than simple physical adsorption

et al. 2015

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a b s t r a c tBacterial colonization and subsequent biofilm formation is still one of the major problems associated with medical devices. Antimicrobial peptides (AMP) immobilization onto biomaterials surface is a promising strategy to avoid bacterial colonization. However, a correct peptide orientation and exposure from the surface is essential to maintain AMP antimicrobial activity.This work aims to evaluate the effect of the immobilization on antibacterial activity of Dhvar5 (LLLFLLKKRKKRKY), an AMP with a head-to-tail amphipathicity. Dhvar5 was linked to thin chitosan coatings in i) a controlled orientation and exposure, testing covalent immobilization of its N-or C-terminus and using spacers with different lengths and flexibilities or in ii) a random orientation by physical adsorption. Chitosan coating was chosen due to its antimicrobial properties and readiness to be functionalized.Surface characterization demonstrated the chemoselective immobilization of the peptide with different spacers in a similar concentration (~2 ng/cm 2 ).Efficacy assays demonstrated that covalent immobilization of Dhvar5 exposing its cationic end, improves the chitosan coating antimicrobial effect by decreasing Methicillin-resistant Staphylococcus aureus (MRSA) colonization. This effect was enhanced when longer spacers were used independently of their flexibility. In opposite, immobilized Dhvar5 exposing its hydrophobic end has no effect on bacterial adhesion to chitosan, and when adsorbed in a random orientation even induces bacterial adhesion to chitosan coating.

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Histatin and lactoferrin derived peptides: Antimicrobial properties and effects on mammalian cells

Cited by 42 publications

References 15 publications

Structure-Activity Relationship Study of Synthetic Variants Derived from the Highly Potent Human Antimicrobial Peptide hLF(1-11)

Structure-Activity Relationship Study of Synthetic Variants Derived from the Highly Potent Human Antimicrobial Peptide hLF(1-11)

Structure-Microbicidal Activity Relationship of Synthetic Fragments Derived from the Antibacterial α-Helix of Human Lactoferrin

Dhvar5 antimicrobial peptide (AMP) chemoselective covalent immobilization results on higher antiadherence effect than simple physical adsorption

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