This is a match-making section for OHAMR Call for proposals 2026.
H - Human Health
A - Animal Health E - EnvironmentP - Plants (Plant Health)biofilm; curli; amyloid; optical tweezers; force spectroscopy
Our lab uses single-molecule force spectroscopy with optical tweezers to examine the folding dynamics of proteins. At the single-molecule limit, probability distributions can be measured directly and are used to derive biophysical mechanisms, examine molecular heterogeneity, and reveal complex protein folding, aggregation and binding mechanisms. Coupled with protein engineering and bioconjugation, we can trap and study single protein molecules or combinations of proteins and binding partners to resolve structural mechanisms that would otherwise be obscured at the ensemble level.
We use optical tweezers to examine the structure and assembly mechanism of functional amyloid (curli) that plays a key role in biofilm structure, in order to define novel antimicrobial targets. Specifically, we have examined CsgA (also with CsgB, CsgC) from Escherichia coli, in monomer and oligomer forms to resolve the initial molecular events of amyloid formation. This approach can be expanded to other biofilm-associated amyloid systems to help define novel structural targets for developing antimicrobials against biofilm-derived pathogens.
Submitted on 2025-11-27 07:11:43
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