Surface-conjugated antimicrobial peptide leucocin a displays high binding to pathogenic gram-positive bacteria.

doi:10.1021/am404729c

Paper

Surface-conjugated antimicrobial peptide leucocin a displays high binding to pathogenic gram-positive bacteria.

Published Jan 8, 2014 · Hashem Etayash, L. Norman, T. Thundat

ACS applied materials & interfaces

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47

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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 μm(2)) compared to 24-residue inactive LeuA fragment (40 ± 8 bacteria/100 μm(2)) 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.

In Vitro Study

Study Snapshot

Leucocin A-functionalized surfaces show high and specific binding to pathogenic gram-positive bacteria, supporting their potential use in antimicrobial peptide-based diagnostic platforms.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Surface-conjugated antimicrobial peptide leucocin a displays high binding to pathogenic gram-positive bacteria.

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References

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The novel multiplex lateral flow assay using antimicrobial peptides can effectively detect and identify three serogroups of Shiga toxin-producing Escherichia coli in food samples at low levels.

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Surface-immobilized 24AA LeuA peptide shows significant binding to Gram-positive bacteria, supporting its potential use as molecular recognition elements in biosensing platforms.

Citations

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