Amino Acid-Modified Conjugated Oligomer Self-Assembly Hydrogel for Efficient Capture and Specific Killing of Antibiotic-Resistant Bacteria.
Qi ZhaoYantao ZhaoZhuanning LuYanli TangPublished in: ACS applied materials & interfaces (2019)
Bacterial infection is one of main causes that threaten global human health. Especially, antibiotic-resistant bacteria like methicillin-resistant Staphylococcus aureus (MRSA) lead to high mortality rate and more expensive treatment cost. Here, a novel amino-acid-modified conjugated oligomer OTE-d-Phe was synthesized by modifying the side chain of conjugated oligo(thiophene ethynylene) with d-phenylalanine. By mixing 9-fluorenylmethyloxycarbonyl-l-phenylalanin (Fmoc-l-Phe) with OTE-d-Phe, a new and biocompatible low-molecular weight hydrogel (HG-2) was prepared through self-assembly. In solution, HG-2 can effectively capture bacteria spontaneously, such as Escherichia coli and MRSA. Most importantly, the hydrogel has specific and strong antibacterial activity against MRSA over methicillin-susceptible S. aureus, Staphylococcus epidermidis, and E. coli. Interestingly, when the hydrogel was put on a model surface, a piece of cloth, it also is able to selectively kill MRSA with low cell cytotoxicity. The antibacterial mechanism was investigated, and it demonstrated that the HG-2 interacts with and physically breaks the cell wall and membrane, which leads to MRSA death. Therefore, this new conjugated oligomer-based hydrogel provides promising applications in disinfection and therapy of MRSA in hospital and in community.
Keyphrases
- methicillin resistant staphylococcus aureus
- staphylococcus aureus
- drug delivery
- escherichia coli
- amino acid
- hyaluronic acid
- human health
- wound healing
- biofilm formation
- photodynamic therapy
- tissue engineering
- risk assessment
- cell wall
- healthcare
- fluorescent probe
- single cell
- type diabetes
- cystic fibrosis
- bone marrow
- living cells
- silver nanoparticles
- pseudomonas aeruginosa
- aqueous solution
- cardiovascular disease
- risk factors
- mass spectrometry
- binding protein