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Journal Article

Quantitative analysis of protease recognition by inhibitors in plasma using microscale thermophoresis

MPS-Authors
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Jenne,  Dieter E.
Emeritus Group: Neuroimmunology / Wekerle, MPI of Neurobiology, Max Planck Society;

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Fulltext (public)

srep35413.pdf
(Publisher version), 666KB

Supplementary Material (public)

srep35413-s1.pdf
(Supplementary material), 17MB

Citation

Dau, T., Edeleva, E. V., Seidel, S. A. I., Stockley, R. A., Braun, D., & Jenne, D. E. (2016). Quantitative analysis of protease recognition by inhibitors in plasma using microscale thermophoresis. Scientific Reports, 6: 35413. doi:10.1038/srep35413.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002C-0A3A-D
Abstract
High abundance proteins like protease inhibitors of plasma display a multitude of interactions in natural environments. Quantitative analysis of such interactions in vivo is essential to study diseases, but have not been forthcoming, as most methods cannot be directly applied in a complex biological environment. Here, we report a quantitative microscale thermophoresis assay capable of deciphering functional deviations from in vitro inhibition data by combining concentration and affinity measurements. We obtained stable measurement signals for the substrate-like interaction of the disease relevant inhibitor alpha-1-antitrypsin (AAT) Z-variant with catalytically inactive elastase. The signal differentiates between healthy and sick AAT-deficient individuals suggesting that affinity between AAT and elastase is strongly modulated by so-far overlooked additional binding partners from the plasma.