Accelerated trypsin autolysis by affinity polymer templates.

ABSTRACT: Self-cleavage of proteins is an important natural process that is difficult to control externally. Recently a new mechanism for the accelerated autolysis of trypsin was discovered involving polyanionic template polymers; however it relies on unspecific interactions and is inactive at elevated salt loads. We have now developed affinity copolymers that bind to the surface of proteases by specific recognition of selected amino acid residues. These are highly efficient trypsin inhibitors with low nanomolar IC₅₀ levels and operate at physiological conditions. In this manuscript we show how these affinity copolymers employ the new mechanism of polymer-assisted self-digest (PAS) and act as a template for multiple protease molecules. Their elevated local concentration leads to accelerat

SUBMITTER: Smolin D 

PROVIDER: S-EPMC9055874 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature