title: Antimicrobial peptide preferential binding of E. coli O157:H7.
abstract: The studies presented here explore antimicrobial peptide preferential binding behavior for a target pathogen, Escherichia coli O157:H7. A modified immunoassay and surface plasmon resonance were employed to evaluate immobilized peptide binding of whole bacterial cells. The knowledge gained may guide the rational design of peptides with enhanced species binding selectivity.
authors.affiliation: Bioscience and Technology Team, US Army Natick Soldier Research, Development, & Engineering Center (NSRDEC), Natick, MA 01760-5020, USA.
authors.forename: Jason W
authors.initials: JW
authors.lastname: Soares
authors.forename: Romy
authors.initials: R
authors.lastname: Kirby
authors.forename: Kimberly M
authors.initials: KM
authors.lastname: Morin
authors.forename: Charlene M
authors.initials: CM
authors.lastname: Mello
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry / Q000378:metabolism*; D002417:Cattle; D019453:Escherichia coli O157 / Q000166:cytology / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D009994:Osmolar Concentration; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D013211:Staphylococcus aureus / Q000378:metabolism; D013379:Substrate Specificity
chemical_list: D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C070016:cecropin P1-LI