Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.
(2016) In ACS Nano 10(1). p.333-341- Abstract
- Characterizing the sizes and interactions of macromolecules under native conditions is a challenging problem in many areas of molecular sciences, which fundamentally arises from the polydisperse nature of biomolecular mixtures. Here, we describe a microfluidic platform for diffusional sizing based on monitoring micron-scale mass transport simultaneously in space and time. We show that the global analysis of such combined space-time data enables the hydrodynamic radii of individual species within mixtures to be determined directly by deconvoluting average signals into the contributions from the individual species. We demonstrate that the ability to perform rapid noninvasive sizing allows this method to be used to characterize interactions... (More)
- Characterizing the sizes and interactions of macromolecules under native conditions is a challenging problem in many areas of molecular sciences, which fundamentally arises from the polydisperse nature of biomolecular mixtures. Here, we describe a microfluidic platform for diffusional sizing based on monitoring micron-scale mass transport simultaneously in space and time. We show that the global analysis of such combined space-time data enables the hydrodynamic radii of individual species within mixtures to be determined directly by deconvoluting average signals into the contributions from the individual species. We demonstrate that the ability to perform rapid noninvasive sizing allows this method to be used to characterize interactions between biomolecules under native conditions. We illustrate the potential of the technique by implementing a single-step quantitative immunoassay that operates on a time scale of seconds and detects specific interactions between biomolecules within complex mixtures. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8504402
- author
- organization
- publishing date
- 2016
- type
- Contribution to journal
- publication status
- published
- subject
- in
- ACS Nano
- volume
- 10
- issue
- 1
- pages
- 9 pages
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- pmid:26678709
- wos:000369115800034
- pmid:26678709
- scopus:84989315217
- ISSN
- 1936-086X
- DOI
- 10.1021/acsnano.5b04713
- language
- English
- LU publication?
- yes
- id
- 08e7bcdb-45d7-432a-b116-5165171d56dc (old id 8504402)
- date added to LUP
- 2016-04-01 10:25:03
- date last changed
- 2023-11-09 20:17:48
@article{08e7bcdb-45d7-432a-b116-5165171d56dc,
abstract = {{Characterizing the sizes and interactions of macromolecules under native conditions is a challenging problem in many areas of molecular sciences, which fundamentally arises from the polydisperse nature of biomolecular mixtures. Here, we describe a microfluidic platform for diffusional sizing based on monitoring micron-scale mass transport simultaneously in space and time. We show that the global analysis of such combined space-time data enables the hydrodynamic radii of individual species within mixtures to be determined directly by deconvoluting average signals into the contributions from the individual species. We demonstrate that the ability to perform rapid noninvasive sizing allows this method to be used to characterize interactions between biomolecules under native conditions. We illustrate the potential of the technique by implementing a single-step quantitative immunoassay that operates on a time scale of seconds and detects specific interactions between biomolecules within complex mixtures.}},
author = {{Arosio, Paolo and Müller, Thomas and Rajah, Luke and Yates, Emma V and Aprile, Francesco A and Zhang, Yingbo and Cohen, Samuel I A and White, Duncan A and Herling, Therese W and De Genst, Erwin J and Linse, Sara and Vendruscolo, Michele and Dobson, Christopher M and Knowles, Tuomas P J}},
issn = {{1936-086X}},
language = {{eng}},
number = {{1}},
pages = {{333--341}},
publisher = {{The American Chemical Society (ACS)}},
series = {{ACS Nano}},
title = {{Microfluidic Diffusion Analysis of the Sizes and Interactions of Proteins under Native Solution Conditions.}},
url = {{http://dx.doi.org/10.1021/acsnano.5b04713}},
doi = {{10.1021/acsnano.5b04713}},
volume = {{10}},
year = {{2016}},
}