Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine.
Controlled protein folding/refolding remains a substantial challenge to the biotechnology industry. Robust and adaptable artificial polymer molecular chaperones could make important contributions towards solving this problem. Taking inspiration from the mechanism of the GroEL/GroES molecular chaperone machine, we report the preparation and testing of a selection of cross-linked thermo-responsive hydrogels, one of which is shown to assist quantitative refolding of a stringent unfolded protein substrate (mitochondrial malate dehydrogenase [mMDH]) during temperature cycling between hydrophobic and hydrophilic states. To our knowledge, this is the first hydrogel-only artificial polymer molecular chaperone to be derived, which is also potentially a generic artificial polymer molecular chaperone for use in a folding bioreactor.
Jones
Huw
H
Imperial College Genetic Therapies Centre, Department of Chemistry, Flowers Building, Imperial College London, UK.
Dalmaris
John
J
Wright
Michael
M
Steinke
Joachim H G
JH
Miller
Andrew D
AD
D018835:Chaperonin 10 / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry*; D020100:Hydrogels; D008958:Models, Molecular; D018716:Molecular Mimicry; D011108:Polymers / Q000737:chemistry*
D018835:Chaperonin 10; D018834:Chaperonin 60; D020100:Hydrogels; D011108:Polymers