Antimicrobial peptide preferential binding of E. coli O157:H7.
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.
Soares
Jason W
JW
Bioscience and Technology Team, US Army Natick Soldier Research, Development, & Engineering Center (NSRDEC), Natick, MA 01760-5020, USA.
Kirby
Romy
R
Morin
Kimberly M
KM
Mello
Charlene M
CM
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
D023181:Antimicrobial Cationic Peptides; D010455:Peptides; C070016:cecropin P1-LI