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- W2789093768 abstract "Short functional peptides are promising materials for use as targeting recognition probes. Toll-like receptor 4 (TLR4) plays an essential role in pathogen recognition and in activation of innate immunity. Here, the TLR4 amino acid sequence was used to screen for bacterial cell binding peptides using a peptide array. Several octamer peptides, including GRHIFWRR, demonstrated binding to Escherichia coli as well as lipopolysaccharides. Linking this peptide with the ZnO-binding peptide HKVAPR, creates a bi-functional peptide capable of one-step ZnO surface modification for bacterial cell entrapment. Ten-fold increase in entrapment of E. coli was observed using the bi-functional peptide. The screened peptides and the simple strategy for nanomaterial surface functionalization can be employed for various biotechnological applications including bacterial cell entrapment onto ZnO surfaces." @default.
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- W2789093768 date "2018-01-01" @default.
- W2789093768 modified "2023-10-18" @default.
- W2789093768 title "Screening of bacteria-binding peptides and one-pot ZnO surface modification for bacterial cell entrapment" @default.
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- W2789093768 doi "https://doi.org/10.1039/c7ra12302g" @default.
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