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- W2017179618 abstract "Leucocin A, a representative class IIa bacteriocin, is a ribosomally synthesized antimicrobial peptide (AMP) that displays potent activity against specific gram-positive bacteria. The antibacterial activity of such peptides is preceded by the binding event that can be utilized for studying specific peptide–bacteria interactions. In this study, 37-residue Leucocin A (LeuA) was synthesized using solid-phase peptide synthesis and covalently immobilized on gold substrates from either the N- or C-terminal. Both the peptide monolayers on gold substrates were incubated separately with five strains of gram-positive bacteria and displayed differential binding to different strains with highest binding to pathogenic Listeria monocytogenes. The C-terminally immobilized LeuA showed higher bacterial binding compared to the N-terminally attached LeuA. The full length immobilized LeuA (37-residue) was active as well as displayed higher bacterial binding (73 ± 6 bacteria/100 μm2) compared to 24-residue inactive LeuA fragment (40 ± 8 bacteria/100 μm2) from the C-terminal region. The high and specific bacterial binding ability of LeuA functionalized surfaces support the potential use of class IIa bacteriocins in antimicrobial peptide-based diagnostic platforms." @default.
- W2017179618 created "2016-06-24" @default.
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- W2017179618 date "2014-01-08" @default.
- W2017179618 modified "2023-10-10" @default.
- W2017179618 title "Surface-Conjugated Antimicrobial Peptide Leucocin A Displays High Binding to Pathogenic Gram-Positive Bacteria" @default.
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- W2017179618 doi "https://doi.org/10.1021/am404729c" @default.
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