Premium
Reversible Deactivation of Enzymes by Redox‐Responsive Nanogel Carriers
Author(s) -
Peng Huan,
Rübsam Kristin,
Jakob Felix,
Pazdzior Patrizia,
Schwaneberg Ulrich,
Pich Andrij
Publication year - 2016
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.201600476
Subject(s) - nanogel , dithiothreitol , chemistry , förster resonance energy transfer , redox , copolymer , aqueous solution , enzyme , cellulase , combinatorial chemistry , polymer chemistry , biophysics , chemical engineering , photochemistry , fluorescence , polymer , organic chemistry , drug delivery , physics , quantum mechanics , engineering , biology
Novel redox‐responsive polymeric nanogels that allow highly efficient enzyme encapsulation and reversible modulation of enzyme activity are developed. The nanogel synthesis and encapsulation of enzyme are performed simultaneously via in situ crosslinking of pyridyldisulfide‐functionalized water‐soluble reactive copolymers, which are synthesized via reversible addition–fragmentation chain transfer copolymerization. Obtained nanogels with loaded cellulase demonstrate very good colloidal stability in aqueous solutions. The enzymatic activity of cellulase is greatly reduced when encapsulated in the nanogels and rapidly recovered in 10 × 10 −3 m dithiothreitol solution. Fluorescence resonance energy transfer (FRET)‐based experiments indicate that the recovered enzymatic activity is mainly ascribed to the release of the enzyme due to the degradation of the disulfide crosslinking network after addition of dithiothreitol (DTT), instead of the enhanced substrate transport rate. The developed enzyme immobilization method opens new possibilities for reversible activation/deactivation of enzymes and opens up new directions for targeted protein therapy and biotechnology applications.