Presentation Title

Towards a Quantitative Understanding of How Artificial Materials Affect Biomolecules

Start Date

November 2016

End Date

November 2016

Location

HUB 302-#45

Type of Presentation

Poster

Abstract

Proteins tend to misfold and adhere to artificial surfaces, limiting our ability to employ proteins and their many functions in technologies. Understanding the physics behind such surface-induced protein misfolding would enable design of improved biocompatible surfaces on which proteins retain their structure and function. Such materials could be used to design new protein-based biosensors for detection of a variety of biomarkers. Thus motivated, I aim to experimentally determine the origins of surface-induced protein adsorption and misfolding using a new, quantitative, technique to measure the thermodynamic stability of surface-tethered proteins. To this end, I have designed, produced, and purified proteins that can be site-specifically attached to surfaces, and characterized their thermodynamic stability in bulk solution. Comparison of the stability of the protein in solution to that of the surface-tethered protein will inform on the effect surfaces have on protein structure and function. Ultimately, I expect my work to lead to the first high-precision measurements of how artificial surfaces affect protein function and stability. These results can then be used to build new, quantitative theoretical models of protein-surface interactions, models that ultimately can be used to guide rational design of new artificial surfaces that are optimally compatible with protein structure and function.

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Nov 12th, 4:00 PM Nov 12th, 5:00 PM

Towards a Quantitative Understanding of How Artificial Materials Affect Biomolecules

HUB 302-#45

Proteins tend to misfold and adhere to artificial surfaces, limiting our ability to employ proteins and their many functions in technologies. Understanding the physics behind such surface-induced protein misfolding would enable design of improved biocompatible surfaces on which proteins retain their structure and function. Such materials could be used to design new protein-based biosensors for detection of a variety of biomarkers. Thus motivated, I aim to experimentally determine the origins of surface-induced protein adsorption and misfolding using a new, quantitative, technique to measure the thermodynamic stability of surface-tethered proteins. To this end, I have designed, produced, and purified proteins that can be site-specifically attached to surfaces, and characterized their thermodynamic stability in bulk solution. Comparison of the stability of the protein in solution to that of the surface-tethered protein will inform on the effect surfaces have on protein structure and function. Ultimately, I expect my work to lead to the first high-precision measurements of how artificial surfaces affect protein function and stability. These results can then be used to build new, quantitative theoretical models of protein-surface interactions, models that ultimately can be used to guide rational design of new artificial surfaces that are optimally compatible with protein structure and function.