Department
Mechanical Engineering
Document Type
Article
Publication Title
eLife
ISSN
2050-084X
DOI
10.7554/eLife.67525
First Page
1
Last Page
20
Publication Date
Fall 1-1-2021
Abstract
Measuring protein-protein interaction (PPI) affinities is fundamental to biochemistry. Yet, conventional methods rely upon the law of mass action and cannot measure many PPIs due to a scarcity of reagents and limitations in the measurable affinity ranges. Here, we present a novel technique that leverages the fundamental concept of friction to produce a mechanical signal that correlates to binding potential. The mechanically transduced immunosorbent (METRIS) assay utilizes rolling magnetic probes to measure PPI interaction affinities. METRIS measures the translational displacement of protein-coated particles on a protein-functionalized substrate. The translational displacement scales with the effective friction induced by a PPI, thus producing a mechanical signal when a binding event occurs. The METRIS assay uses as little as 20 pmols of reagents to measure a wide range of affinities while exhibiting a high resolution and sensitivity. We use METRIS to measure several PPIs that were previously inaccessible using traditional methods, providing new insights into epigenetic recognition.
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Recommended Citation
Steimel, J. P.,
Harrison, J.,
Strahl, B.,
Sandoval, D.,
Pappas, M.,
Randene, K.,
&
Petell, C.
(2021).
Mechanically transduced immunosorbent assay to measure protein-protein interactions.
eLife, , 1–20.
DOI: 10.7554/eLife.67525
https://scholarlycommons.pacific.edu/soecs-facarticles/221
