Literature DB >> 22995710

Arginine-rich self-assembling peptides as potent antibacterial gels.

Ana Salomé Veiga1, Chomdao Sinthuvanich, Diana Gaspar, Henri G Franquelim, Miguel A R B Castanho, Joel P Schneider.   

Abstract

Hydrogel materials that display inherent activity against bacteria can be used to directly treat accessible wounds to prevent or kill existing infection. Hydrogels composed of self-assembling β-hairpin peptides, having a high content of arginine, were found to be extremely effective at killing both gram-positive and gram-negative bacteria, including multi-drug resistant Pseudomonas aeruginosa. No added antibacterial agents are necessary to realize activity. Using self-assembling peptides for material construction allows facile structure-activity relationships to be determined since changes in peptide sequence at the monomer level are directly transposed to the bulk material's antibacterial properties. SAR studies show that arginine content largely influences the hydrogel's antibacterial activity, and influences their bulk rheological properties. These studies culminated in an optimized gel, composed of the peptide PEP6R (VKVRVRVRV(D)PPTRVRVRVKV). PEP6R gels prepared at 1.5 wt % or higher concentration, demonstrate high potency against bacteria, but are cytocompatible toward human erythrocytes as well as mammalian mesenchymal stem cells. Rheological studies indicate that the gel is moderately stiff and displays shear-thin recovery behavior, allowing its delivery via simple syringe. Published by Elsevier Ltd.

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Year:  2012        PMID: 22995710      PMCID: PMC3466390          DOI: 10.1016/j.biomaterials.2012.08.046

Source DB:  PubMed          Journal:  Biomaterials        ISSN: 0142-9612            Impact factor:   12.479


  30 in total

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Review 4.  Cationic antiseptics: diversity of action under a common epithet.

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Review 6.  Hospital epidemiology and infection control in acute-care settings.

Authors:  Emily R M Sydnor; Trish M Perl
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7.  Injectable solid hydrogel: mechanism of shear-thinning and immediate recovery of injectable β-hairpin peptide hydrogels.

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10.  Structure-activity determinants in paneth cell alpha-defensins: loss-of-function in mouse cryptdin-4 by charge-reversal at arginine residue positions.

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  39 in total

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Review 7.  Antimicrobial hydrogels: promising materials for medical application.

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8.  Design of self-assembling peptide hydrogelators amenable to bacterial expression.

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9.  Switching the Immunogenicity of Peptide Assemblies Using Surface Properties.

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10.  Self-assembly of cationic multidomain peptide hydrogels: supramolecular nanostructure and rheological properties dictate antimicrobial activity.

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