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Charge-Mediated Co-assembly of Amphiphilic Peptide and Antibiotics Into Supramolecular Hydrogel With Antibacterial Activity
- Source :
- Frontiers in Bioengineering and Biotechnology, Vol 8 (2020)
- Publication Year :
- 2020
- Publisher :
- Frontiers Media S.A., 2020.
-
Abstract
- Bacteria are the most common pathogens to cause infection of surgical sites, which usually induce severe postoperative morbidity and more healthcare costs. Inhibition of bacteria adhesion and colonization is an effective strategy to prevent the spread of infection at the surgical sites. Hydrogels have been widely used as promising antibacterial materials, due to their unique porous structure that could accommodate various antibacterial agents (e.g., antibiotics and cationic polymers with inherent antibacterial activity). Herein, inspired by the natural protein self-assembly, an amphiphilic peptide comprised of a hydrophobic naphthyl (Nap) acetyl tail and a hydrophilic peptide backbone was employed to construct supramolecular hydrogel for sustained release of the antibiotic polymyxin B. At neutral pH, the negatively charged amphiphilic peptide could form electrostatic attraction interaction with the positively charged polymyxin B, which could thus drive the ionized peptide molecules to get close to each other and subsequently trigger the self-assembly of the amphiphilic peptide into supramolecular hydrogel via intermolecular hydrogen bonding interaction among the peptide backbones and π-stacking of the hydrophobic Nap tails. More importantly, the electrostatic attraction interaction between polymyxin B and the amphiphilic peptide could ensure the sustained release of polymyxin B from the supramolecular hydrogel, leading to an effective inhibition of Gram-negative bacteria Escherichia coli growth. Combining the good biocompatibility of the amphiphilic peptide, the supramolecular hydrogel developed in this work shows a great potential for the surgical site infection application.
Details
- Language :
- English
- ISSN :
- 22964185
- Volume :
- 8
- Database :
- Directory of Open Access Journals
- Journal :
- Frontiers in Bioengineering and Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.287df1e5732478f89631038987743c2
- Document Type :
- article
- Full Text :
- https://doi.org/10.3389/fbioe.2020.629452