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@article{2251352,
author = {Yang, Tianjin and Villois, Alessia and Kunka, Antonín and Grigolato, Fulvio and Arosio, Paolo and Prokop, Zbyněk and deMello, Andrew and Stavrakis, Stavros},
article_number = {48},
doi = {http://dx.doi.org/10.1021/acs.analchem.2c03009},
keywords = {Biotechnology; Fluid dynamics; Kinetics; Liquids; Nanofibers},
language = {eng},
issn = {0003-2700},
journal = {Analytical chemistry},
title = {Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics},
url = {https://doi.org/10.1021/acs.analchem.2c03009},
volume = {94},
year = {2022}
}
TY - JOUR
ID - 2251352
AU - Yang, Tianjin - Villois, Alessia - Kunka, Antonín - Grigolato, Fulvio - Arosio, Paolo - Prokop, Zbyněk - deMello, Andrew - Stavrakis, Stavros
PY - 2022
TI - Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics
JF - Analytical chemistry
VL - 94
IS - 48
SP - 16675-16684
EP - 16675-16684
PB - American Chemical Society
SN - 00032700
KW - Biotechnology
KW - Fluid dynamics
KW - Kinetics
KW - Liquids
KW - Nanofibers
UR - https://doi.org/10.1021/acs.analchem.2c03009
N2 - Protein folding, unfolding, and aggregation are important in a variety of biological processes and intimately linked to “protein misfolding diseases”. The ability to perform experiments at different temperatures allows the extraction of important information regarding the kinetics and thermodynamics of such processes. Unfortunately, conventional stopped-flow methods are difficult to implement, generate limited information, and involve complex sample handling. To address this issue, we present a temperature-controlled droplet-based microfluidic platform that allows measurement of reaction kinetics on millisecond to second timescales and at temperatures between ambient and 90 °C. The utility of the microfluidic platform for measuring fast biomolecular kinetics at high temperatures is showcased through the investigation of the unfolding kinetics of haloalkane dehalogenases and the elongation of fibrils composed of the amyloid β peptide associated with Alzheimer’s disease. In addition, a deep-ultraviolet (UV) fluorescence microscope was developed for the on-chip recording of protein intrinsic fluorescence spectrum originating from aromatic amino acid residues. We envision that the developed optofluidic platform will find wide applicability in the analysis of biological processes, such as protein refolding and phase separation.
ER -
YANG, Tianjin, Alessia VILLOIS, Antonín KUNKA, Fulvio GRIGOLATO, Paolo AROSIO, Zbyněk PROKOP, Andrew DEMELLO a Stavros STAVRAKIS. Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics. \textit{Analytical chemistry}. American Chemical Society, 2022, roč.~94, č.~48, s.~16675-16684. ISSN~0003-2700. Dostupné z: https://dx.doi.org/10.1021/acs.analchem.2c03009.
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