2022
Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics
YANG, Tianjin, Alessia VILLOIS, Antonín KUNKA, Fulvio GRIGOLATO, Paolo AROSIO et. al.Základní údaje
Originální název
Droplet-Based Microfluidic Temperature-Jump Platform for the Rapid Assessment of Biomolecular Kinetics
Autoři
YANG, Tianjin, Alessia VILLOIS, Antonín KUNKA (203 Česká republika, domácí), Fulvio GRIGOLATO, Paolo AROSIO, Zbyněk PROKOP (203 Česká republika, garant, domácí), Andrew DEMELLO a Stavros STAVRAKIS
Vydání
Analytical chemistry, American Chemical Society, 2022, 0003-2700
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10400 1.4 Chemical sciences
Stát vydavatele
Spojené státy
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 7.400
Kód RIV
RIV/00216224:14310/22:00128417
Organizační jednotka
Přírodovědecká fakulta
UT WoS
000888138400001
Klíčová slova anglicky
Biotechnology; Fluid dynamics; Kinetics; Liquids; Nanofibers
Štítky
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 31. 1. 2023 08:46, Mgr. Marie Šípková, DiS.
Anotace
V originále
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.
Návaznosti
EF17_043/0009632, projekt VaV |
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857560, interní kód MU (Kód CEP: EF17_043/0009632) |
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