Thermodynamic characterization of amyloid polymorphism by microfluidic transient incomplete separation.

ABSTRACT: Amyloid fibrils of proteins such as α-synuclein are a hallmark of neurodegenerative diseases and much research has focused on their kinetics and mechanisms of formation. The question as to the thermodynamic stability of such structures has received much less attention. Here, we newly utilize the principle of transient incomplete separation of species in laminar flow in combination with chemical depolymerization for the quantification of amyloid fibril stability. The relative concentrations of fibrils and monomer at equilibrium are determined through an in situ separation of these species based on their different diffusivity inside a microfluidic capillary. The method is highly sample economical, using much less than a microliter of sample per data point and its only requirement is t

SUBMITTER: Farzadfard A 

PROVIDER: S-EPMC10866369 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature