title: Rapid detection of pathogenic bacteria and screening of phage-derived peptides using microcantilevers.
abstract: We report the use of an array of microcantilevers to measure the specific binding of Salmonella to peptides derived from phage display libraries. Selectivity of these phage-derived peptides for Salmonella spp. and other pathogens ( Listeria monocytogenes and Escherichia coli ) are compared with a commercially available anti- Salmonella antibody and the antimicrobial peptide alamethicin. A Langmuir isotherm model was applied to determine the binding affinity constants of the peptides to the pathogens. One particular peptide, MSal 020417, demonstrated a higher binding affinity to Salmonella spp. than the commercially available antibody and is able to distinguish among eight Salmonella serovars on a microcantilever. A multiplexed screening system to quickly determine the binding affinities of various peptides to a particular pathogen highly improves the efficiency of the peptide screening process. Combined with phage-derived peptides, this microcantilever-based technique provides a novel biosensor to rapidly and accurately detect pathogens and holds potential to be further developed as a screening method to identify pathogen-specific recognition elements.
authors.affiliation: Department of Chemical and Biomolecular Engineering, Rice University , Houston, Texas 77005, United States.
authors.forename: Jinghui
authors.initials: J
authors.lastname: Wang
authors.forename: Mary Josephine
authors.initials: MJ
authors.lastname: McIvor
authors.forename: Christopher T
authors.initials: CT
authors.lastname: Elliott
authors.forename: Nitsara
authors.initials: N
authors.lastname: Karoonuthaisiri
authors.forename: Laura
authors.initials: L
authors.lastname: Segatori
authors.forename: Sibani Lisa
authors.initials: SL
authors.lastname: Biswal
mesh_terms: D000595:Amino Acid Sequence; D001419:Bacteria / Q000302:isolation & purification* / Q000378:metabolism; D015374:Biosensing Techniques / Q000379:methods*; D055616:Microtechnology / Q000379:methods*; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry / Q000378:metabolism*; D013045:Species Specificity; D013499:Surface Properties; D013997:Time Factors
chemical_list: D019151:Peptide Library; D010455:Peptides