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|Tucker, Matthew J
|Date of Issue
|The protein-structure function relation is crucial to biological processes. Misfolding of peptides and proteins can give rise to possible ailments and even death. Besides maintaining biological function, the structure of peptides can also influence the way they interact in a membrane environment. AMPs are a class of peptides that exhibit selectiveness in disrupting biological function of pathogens. Though many mechanisms exist for AMPs to kill pathogens, the most common mode of action is by disruption of the lipid protection, either cell membrane or viral envelope, of the pathogen. Being able to tune the selectivity and activity of AMPs would increase the chances of being able to selectively target pathogens while minimizing unwanted cytotoxicity against healthy cells. In order to be understand and be able to tune these features, spectroscopic studies analyzing binding affinities and the secondary structure changes of AMPs upon membrane binding have been performed. Additionally, new derivatives of APEG membrane models are reported and characterized.
|Enlightenment via Spectroscopy: Monitoring Antimicrobial Peptide-Membrane Interactions of Bombolitins and MP1
|Wallace, Ian S
|White, Thomas G
|Williams, Joshua B
|Leitner, David M