Abstract

Nisin is a cationic amphiphilic peptide consisting of 34 amino acids with a cluster of hydrophobic residues at the N-terminus and hydrophilic residues at the C-terminus. The mechanism of its action is based on its ability to attach to the bacteria cell membrane before to then cause cell lysis. This antimicrobial peptide was used as biological molecule for the development of a novel impedimetric label-free biosensor for the monitoring of bacterial contamination. The binding affinities of Nisin immobilized with its N-terminus and C-terminus were compared, highlighting the capability of the last configuration to obtain the best analytical performance of the developed biosensor when non-pathogenic Escherichia Coli O157:H7 and Listeria innocua cells were investigated.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.