Single molecule resolution of peptide-lipopolysaccharide interactions (8.3, Microbial Physiology and Engineering)
Abstract
Host-defense peptides, including cationic antimicrobial peptides (AMPs) represent a ubiquitous defense mechanism against bacterial infection by disrupting the bacterial cell membrane and/or modulating toxic/inflammatory responses toward bacterial components. This study will directly compare the dynamic interactions of AMPs with native bacterial lipopolysaccharide (LPS) components found in the bacterial membrane and with aminoarabinose- or glucosamine-modified LPS produced by specific bacterial strains. Physical platforms will be developed to study dynamic interactions of LPS (or LPS components) on peptide-decorated surfaces and of peptides on supported lipid bilayers containing LPS. These platforms will be validated using surface-specific analytical methods and ensemble affinity measurements. Single-molecule tracking methods will be developed to measure the specific rates associated with adsorption and desorption between the peptides and the LPS species. Single-molecule FRET methods will then be used to identify and measure binding events between individual peptide-LPS pairs.
Document Details
- Document Type
- DoD Grant Award
- Publication Date
- Jan 12, 2017
- Source ID
- W911NF1610151
Entities
People
- Daniel K. Schwartz
Organizations
- Army Contracting Command
- United States Army
- University of Colorado Boulder