Lectin-Functionalized Composite Hydrogels for "Capture-and-Killing" of Carbapenem-Resistant Pseudomonas aeruginosa.
Nicholas BodenbergerDennis KubiczekDaniel HalbgebauerVittoria RimolaSebastian WieseDaniel MayerArmando Alexei Rodriguez AlfonsoLudger StändkerSteffen StengerFrank RosenauPublished in: Biomacromolecules (2018)
Infections with multiresistant pathogens are a leading cause for mortality worldwide. Just recently, the World Health Organization (WHO) increased the threat rating for multiresistant Pseudomonas aeruginosa to the highest possible level. With this background, it is crucial to develop novel materials and procedures in the fight against multiresistant pathogens. In this study, we present a novel antimicrobial material, which could find applications as a wound dressing or antimicrobial coating. Lectins are multivalent sugar-binding proteins, which can be found in a variety of plants and bacteria, where they are associated with biofilm formation. By immobilizing lectin B on a protein-based hydrogel surface, we provided the hydrogel with the ability to immobilize ("catch") pathogens upon contact. Furthermore, another hydrogel layer was added which inhibits biofilm formation and releases a highly potent antimicrobial peptide to eradicate microorganisms ("kill"). The composite hydrogel showed a high antimicrobial activity against the reference strain Pseudomonas aeruginosa PAO1 as well as against a carbapenem-resistant clinical isolate (multiresistant Gram-negative class 4) and may thus represent a novel material to develop a new type of antimicrobial wound dressings to prevent infections with this problematic pathogen of burn or other large wounds.
Keyphrases
- biofilm formation
- wound healing
- gram negative
- pseudomonas aeruginosa
- staphylococcus aureus
- multidrug resistant
- drug delivery
- cystic fibrosis
- candida albicans
- hyaluronic acid
- acinetobacter baumannii
- tissue engineering
- escherichia coli
- drug resistant
- antimicrobial resistance
- type diabetes
- low density lipoprotein
- binding protein
- quantum dots
- mass spectrometry
- small molecule
- amino acid
- surgical site infection