Antimicrobial activities of heparin‐binding peptides

Andersson, Emma; Rydengård, Victoria; Sonesson, Andreas; Mörgelin, Matthias; Björck, Lars; Schmidtchen, Artur

doi:10.1111/j.1432-1033.2004.04035.x

Cited by 171 publications

(167 citation statements)

References 56 publications

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“…C3a caused local perturbations and breaks along P. aeruginosa plasma membranes, and occasionally, intracellular material was found extracellularly. These findings were similar to those seen after treatment with the AMP LL-37 (13). To further analyze the effects of C3a on membranes, we used a liposome model to study membrane binding and permeabilisation (Fig.…”

Section: Resultsmentioning

confidence: 50%

“…1C). As recently shown, amphipaticity, cationicity, and helix structure are features that characterize heparinbinding peptides but also confer antimicrobial properties to this group of molecules (13). Therefore, the finding that C3a interacts with heparin at physiological conditions provides an additional link between C3a and many cationic AMPs.…”

Section: Resultsmentioning

confidence: 94%

“…3D). The binding of heparin to peptides LRK26 and LGE27 has been presented (13) but is shown here for completeness. Three peptides (LRK26, LGE27, and CNY21) were labeled with the fluorescent dye TAMRA and incubated with P. aeruginosa.…”

Section: Resultsmentioning

confidence: 99%

“…Concentrations killing 80-100% of E. faecalis were 3-6 M for LRK26, LGE27 (presented in ref. 13) and CNY21. LTE21 was less effective against this bacterium, and LGL5 showed no antimicrobial activity at all.…”

Section: Resultsmentioning

confidence: 99%

“…C3a, C3a-desArg, C3 (2 g), and the synthetic peptides (1, 2, and 5 g) were applied onto nitrocellulose membranes (Hybond-C, Amersham Biosciences). Membranes were blocked (PBS, pH 7.4͞3% BSA) for 1 h and incubated with radiolabeled heparin (Ϸ10 g͞ml) (13). Unlabeled heparin (6 mg͞ml) was added for competition of binding (Fig.…”

Section: Methodsmentioning

confidence: 99%

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Activation of the complement system generates antibacterial peptides

Nordahl

Rydengård

Nyberg

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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211

174

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The complement system represents an evolutionary old and significant part of the innate immune system involved in protection against invading microorganisms. Here, we show that the anaphylatoxin C3a and its inactivated derivative C3a-desArg are antibacterial, demonstrating a previously unknown direct antimicrobial effect of complement activation. The C3a peptide, as well as functional epitopes in the sequence, efficiently killed the Gramnegative bacteria Escherichia coli, Pseudomonas aeruginosa, and the Gram-positive Enterococcus faecalis. In mice, a C3a-derived peptide suppressed infection by Gram-positive Streptococcus pyogenes bacteria. Fluorescence and electron microscopy demonstrated that C3a binds to and induces breaks in bacterial membranes. C3a was also found to induce membrane leakage of liposomes. These findings provide an interesting link between the complement system and antimicrobial peptides, which are two important branches of innate immunity.bacteria ͉ inflammation ͉ innate immunity

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Section: Resultsmentioning

confidence: 50%

Section: Resultsmentioning

confidence: 94%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 3 more Smart Citations

Activation of the complement system generates antibacterial peptides

Nordahl

Rydengård

Nyberg

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

211

174

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Antimicrobial Materials for Medical Devices

Szycher

2015

Kirk-Othmer Encyclopedia of Chemical Technology

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Antimicrobial materials and technologies, including antimicrobial polymers and polymeric biocides, silver, and copper antimicrobial technologies, and antimicrobial textiles exhibit antimicrobial activity: the ability to inhibit the growth of pathogenic microorganisms such as bacteria, fungi, yeast, and algae. The design and application of antimicrobial materials is a rapidly growing field. There is an urgent need for infection prevention strategies that do not require the use of antibiotics, which exacerbate the rise of multidrug‐ and pan‐drug‐resistant infectious microorganisms, particularly in the medical field. The article presents antimicrobial polymeric systems, their mechanism of action, and various applications for medical and health care use: industrial, agricultural, architectural, heating, ventilation, and air‐conditioning (HVAC), and consumer goods. Related aspects of antimicrobial resistance, multidrug‐resistant organisms, and biofouling are also discussed.

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The bacteriolytic activity of native and covalently immobilized lysozyme against Gram‐positive and Gram‐negative bacteria is differentially affected by charged amino acids and glycine

et al. 2019

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The emergence of new antibiotic‐resistant bacterial strains means it is increasingly important to find alternatives to traditional antibiotics, such as bacteriolytic enzymes. The bacteriolytic enzyme lysozyme is widely used in medicine as an antimicrobial agent, and covalent immobilization of lysozyme can expand its range of possible applications. However, information on the effect of such immobilized preparations on whole bacterial cells is quite limited. Here, we demonstrate the differential effects of glycine and charged (basic and acidic) amino acids on the enzymatic lysis of Gram‐positive and Gram‐negative bacteria by soluble and immobilized lysozyme. Glycine and basic amino acids (histidine, lysine, and arginine) significantly increase the rate of lysis of Gram‐negative Escherichia coli cells in the presence of soluble lysozyme, but they do not substantially affect the rate of enzymatic lysis of Gram‐positive Micrococcus luteus . Glutamate and aspartate significantly enhance enzymatic lysis of both E. coli and M. luteus . When using immobilized lysozyme, the effects of amino acids on the rate of cell lysis are significantly reduced. For immobilized lysozyme, the presence of an external diffusion mode on cell lysis kinetics at bacterial concentrations below 4 × 10 8 colony‐forming units·mL −1 was shown. The broadening of the pH optimum of lysozyme activity after immobilization has been demonstrated for both Gram‐positive and Gram‐negative bacteria. The Michaelis constant ( K m ) values of immobilized lysozyme were increased by 1.5‐fold for E. coli cell lysis and 4.6‐fold for M. luteus cell lysis compared to soluble enzyme. A greater understanding of the effect of amino acids on the activity of native and immobilized lysozyme is important for both the development of new materials for medical purposes and elucidating the interaction of lysozyme with bacterial cells. Of particular interest is our finding that lysozyme activity against Gram‐negative bacteria is enhanced in the presence of glycine and charged amino acids over a wide range of concentrations.

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Antimicrobial activities of heparin‐binding peptides

Cited by 171 publications

References 56 publications

Activation of the complement system generates antibacterial peptides

Activation of the complement system generates antibacterial peptides

Antimicrobial Materials for Medical Devices

The bacteriolytic activity of native and covalently immobilized lysozyme against Gram‐positive and Gram‐negative bacteria is differentially affected by charged amino acids and glycine

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