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Quantitative analysis of protease recognition by inhibitors in plasma using microscale thermophoresis.
Sci. Rep. 6:35413 (2016)
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 α-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.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
Neutrophil Elastase; Living Cells; Alpha(1)-antitrypsin; Mechanism; Alpha-1-antitrypsin; Progression; Deficiency; Activation; Insights; Linking
ISSN (print) / ISBN
2045-2322
e-ISSN
2045-2322
Journal
Scientific Reports
Quellenangaben
Volume: 6,
Article Number: 35413
Publisher
Nature Publishing Group
Publishing Place
London
Non-patent literature
Publications
Reviewing status
Peer reviewed
Institute(s)
Institute of Lung Health and Immunity (LHI)