title: Hydrogel polymer appears to mimic the performance of the GroEL/GroES molecular chaperone machine.
abstract: 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.
authors.affiliation: Imperial College Genetic Therapies Centre, Department of Chemistry, Flowers Building, Imperial College London, UK.
authors.forename: Huw
authors.initials: H
authors.lastname: Jones
authors.forename: John
authors.initials: J
authors.lastname: Dalmaris
authors.forename: Michael
authors.initials: M
authors.lastname: Wright
authors.forename: Joachim H G
authors.initials: JH
authors.lastname: Steinke
authors.forename: Andrew D
authors.initials: AD
authors.lastname: Miller
mesh_terms: D018835:Chaperonin 10 / Q000737:chemistry*; D018834:Chaperonin 60 / Q000737:chemistry*; D020100:Hydrogels; D008958:Models, Molecular; D018716:Molecular Mimicry; D011108:Polymers / Q000737:chemistry*
chemical_list: D018835:Chaperonin 10; D018834:Chaperonin 60; D020100:Hydrogels; D011108:Polymers