Full Thermal Switching of Enzymes by Thermoresponsive Poly(2‐oxazoline)‐Based Enzyme Inhibitors

Abstract

Controlling the activity of enzymes is an important feature for many processes in medicine, bioanalytics, and biotechnology.S of ar,i th as not been possible to fully switch biocatalystso na nd off by thermoresponsive enzymei nhibitors. Herein, we presentp oly(2-oxazoline)s with iminodiacetic acide nd groups (POx-IDA) that are lower critical solution temperature (LCST) polymers and thus thermosensitive. They are capableo fr eversibly inhibiting the activity of horse radish peroxidase and laccaseb y more than 99 %. Increasingt he temperature makes the POx-IDAp recipitate, which leads to 100 %r ecovery of the enzymea ctivity. This switching cycle is fully reversible.T he LCST of the POx-IDA can be tuned by varying the polymer composition to generate aw ide range of switching windows.

Effect of Dexamethasone on Thermoresponsive Behavior of Poly(2-Oxazoline) Diblock Copolymers

“…The thermoresponsive part served as a stabilizing interlayer between the charged core and the hydrophilic corona. An unusual application of thermoresponsive polymers was presented by Tiller et al [ 36 ], where thermoresponsive POx containing iminodiacetic acid end groups (POx-IDA) were employed as reversible enzyme activity thermal switches of horseradish peroxidase and laccase. At the temperature below T cp , they were able to inhibit the activity of horseradish peroxidase and laccase by more than 99%.…”