| Literature DB >> 27477869 |
Roshan C Dalpadado1, Hendrik Maat1, John A Carver1, Damien Hall2.
Abstract
We demonstrate the real-time monitoring of the growth of amyloid-protein aggregates in a semi-rigid gel environment constructed from a 5% w/v gelatin solution. The kinetics of amyloid fibril growth from reduced and carboxy-methylated κ-casein occurring in the gel medium was contrasted against that obtained in a regular solution assay. Aggregation kinetics were recorded using Thioflavin T fluorescence. Transmission electron microscopy was used to confirm the aggregates' existence and morphology. The current demonstration of controlled amyloid growth in a gel environment represents the first step towards development of an experimental model for investigating the role of spatial and medium factors in the kinetics of aggregation-based proteopathies. CrownEntities:
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Year: 2016 PMID: 27477869 DOI: 10.1016/j.ab.2016.07.024
Source DB: PubMed Journal: Anal Biochem ISSN: 0003-2697 Impact factor: 3.365