Unknown

Dataset Information

0

Quantifying Biomolecular Binding Constants using Video Paper Analytical Devices.


ABSTRACT: A novel ultra-low-cost biochemical analysis platform to quantify protein dissociation binding constants and kinetics using paper microfluidics is reported. This approach marries video imaging with one of humankind's oldest materials: paper, requiring no large, expensive laboratory equipment, complex microfluidics or external power. Temporal measurements of nanoparticle-antibody conjugates binding on paper is found to follow the Langmuir Adsorption Model. This is exploited to measure a series of antibody-antigen dissociation constants on paper, showing excellent agreement with a gold-standard benchtop interferometer. The concept is demonstrated with a camera and low-end smartphone, 500-fold cheaper than the reference method, and can be multiplexed to measure ten reactions in parallel. These findings will help to widen access to quantitative analytical biochemistry, for diverse applications spanning disease diagnostics, drug discovery, and environmental analysis in resource-limited settings.

SUBMITTER: Miller BS 

PROVIDER: S-EPMC6055620 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Quantifying Biomolecular Binding Constants using Video Paper Analytical Devices.

Miller Benjamin S BS   Parolo Claudio C   Turbé Valérian V   Keane Candice E CE   Gray Eleanor R ER   McKendry Rachel A RA  

Chemistry (Weinheim an der Bergstrasse, Germany) 20180608 39


A novel ultra-low-cost biochemical analysis platform to quantify protein dissociation binding constants and kinetics using paper microfluidics is reported. This approach marries video imaging with one of humankind's oldest materials: paper, requiring no large, expensive laboratory equipment, complex microfluidics or external power. Temporal measurements of nanoparticle-antibody conjugates binding on paper is found to follow the Langmuir Adsorption Model. This is exploited to measure a series of  ...[more]

Similar Datasets

| S-EPMC3852662 | biostudies-literature
| S-EPMC3931572 | biostudies-literature
| S-EPMC5701284 | biostudies-literature
| S-EPMC5543161 | biostudies-other
| S-EPMC7450514 | biostudies-literature
| S-EPMC3979282 | biostudies-literature
| S-EPMC6030327 | biostudies-literature
| S-EPMC7071557 | biostudies-literature
| S-EPMC5975359 | biostudies-literature
| S-EPMC10499984 | biostudies-literature