Title

Mechanically Transduced Immunosorbent Assay

Poster Number

14

Lead Author Major

Bioengineering

Lead Author Status

Senior

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

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Apr 24th, 1:00 PM Apr 24th, 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.