Mechanically Transduced Immunosorbent Assay
Poster Number
14
Format
Poster Presentation
Faculty Mentor Name
Joshua Steimel
Faculty Mentor Department
School of Engineering and Computer Science, Mechanical Engineering Department
Abstract/Artist Statement
Measuring biological interaction affinities, particularly protein-protein interactions (PPI), is essential to biochemistry. Despite this, many critical interactions are unmeasurable because of limitations in the affinity ranges that can be measured or simply a lack of reagents. Here we present a novel technique to measure PPI interaction affinities by utilizing rolling magnetic probes (RMP) and the concept friction that is induced by these binding interactions. RMP measures the translational displacement of protein-coated particles on a protein-functionalized substrate that is induced by the increase in friction due to the strength and density of these biological interactions. This translational displacement correlates with the effective friction that is induced by the biological interaction. This produces a mechanical signal which indicates binding. RMP is capable of measuring interactions across a wide range of affinities, 10−3−10−15M, has high resolution, measures ΔΔG differences of about 0.4 kcalmol, and also uses a small amount of reagents, 20 pmol. Here, RMP provides quantitative insights into the interplay between epigenetic modifications.
Location
University of the Pacific, 3601 Pacific Ave., Stockton, CA 95211
Start Date
24-4-2021 1:00 PM
End Date
24-4-2021 2:15 PM
Mechanically Transduced Immunosorbent Assay
University of the Pacific, 3601 Pacific Ave., Stockton, CA 95211
Measuring biological interaction affinities, particularly protein-protein interactions (PPI), is essential to biochemistry. Despite this, many critical interactions are unmeasurable because of limitations in the affinity ranges that can be measured or simply a lack of reagents. Here we present a novel technique to measure PPI interaction affinities by utilizing rolling magnetic probes (RMP) and the concept friction that is induced by these binding interactions. RMP measures the translational displacement of protein-coated particles on a protein-functionalized substrate that is induced by the increase in friction due to the strength and density of these biological interactions. This translational displacement correlates with the effective friction that is induced by the biological interaction. This produces a mechanical signal which indicates binding. RMP is capable of measuring interactions across a wide range of affinities, 10−3−10−15M, has high resolution, measures ΔΔG differences of about 0.4 kcalmol, and also uses a small amount of reagents, 20 pmol. Here, RMP provides quantitative insights into the interplay between epigenetic modifications.