November 18, 2013
Understanding the effect of near-surface environments on protein conformation is critical in many fields, including biosensing, cell culture, tissue engineering, biocatalysis, and pharmaceutical formulation.
The research groups of Assistant Professor Joel Kaar and Professor Dan Schwartz have been investigating a novel technique to characterize changes in protein structure on surfaces; their research on the subject was recently published in the Proceedings of the National Academy of Sciences (PNAS).
Along with Kaar and Schwartz, co-authors include Assistant Research Professor Mark Kastantin and Research Associate Sean McLoughlin.
In their paper, the researchers describe a unique approach to characterizing dynamic changes in protein structure in near-surface environments using dynamic single-molecule microscopy. This approach specifically exploits Förster resonance energy transfer (FRET) tracking to elucidate changes in protein structure on surfaces at the single-molecule level.
Using this approach, structural changes in the model enzyme organophosphorus hydrolase were monitored upon adsorption to fused silica on a molecule-by-molecule basis.
This method, which is widely applicable to virtually any protein, provides the framework for developing surfaces and surface modifications with improved biocompatibility.