1. Department of Pharmaceutics, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands;2. Department of Medicinal Chemistry and Chemical Biology, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, P.O. Box 80082, 3508 TB Utrecht, The Netherlands;3. Biomolecular Mass Spectrometry and Proteomics Group, Bijvoet Center for Biomolecular Research, Utrecht Institute for Pharmaceutical Sciences, Utrecht University, Padualaan 8, 3584 CH, The Netherlands
Abstract:
An efficient strategy is reported to introduce methacrylamide groups on the lysine residues of a model protein (lysozyme) for immobilization and triggered release from a hydrogel network. A novel spacer unit was designed, containing a disulfide bond, such that the release of the protein can be triggered by reduction. The modified proteins were characterized by MALDI‐TOF MS, titration of free NH2 residues and spectral analysis. The modification reaction is well controlled, and the number of introduced functions can be tailored by changing the reaction conditions. Gel electrophoresis experiments showed that the methacrylamide modified protein can be immobilized in a polyacrylamide hydrogel and subsequently released by reduction of the spacer by which the protein was grafted to the polymeric network.
