Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the protein

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Semenyuk , P , Tiainen , T , Hietala , S , Tenhu , H , Aseyev , V & Muronetz , V 2019 , ' Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the protein ' , International Journal of Biological Macromolecules , vol. 121 , pp. 536-545 . https://doi.org/10.1016/j.ijbiomac.2018.10.031

Title: Artificial chaperones based on thermoresponsive polymers recognize the unfolded state of the protein
Author: Semenyuk, Pavel; Tiainen, Tony; Hietala, Sami; Tenhu, Heikki; Aseyev, Vladimir; Muronetz, Vladimir
Contributor organization: Department of Chemistry
Vladimir Aseyev / Principal Investigator
Date: 2019-01
Language: eng
Number of pages: 10
Belongs to series: International Journal of Biological Macromolecules
ISSN: 0141-8130
DOI: https://doi.org/10.1016/j.ijbiomac.2018.10.031
URI: http://hdl.handle.net/10138/306073
Abstract: Stabilization of the enzymes under stress conditions is of special interest for modern biochemistry, bioengineering, as well as for formulation and target delivery of protein-based drugs. Aiming to achieve an efficient stabilization at elevated temperature with no influence on the enzyme under normal conditions, we studied chaperone-like activity of thermoresponsive polymers based on poly(dimethylaminoethyl methacrylate) (PDMAEMA) toward two different proteins, glyceraldehyde-3-phosphate dehydrogenase and chicken egg lysozyme. The polymers has been shown to do not interact with the folded protein at room temperature but form a complex upon heating to either protein unfolding or polymer phase transition temperature. A PDMAEMA-PEO block copolymer with a dodecyl end-group (d-PDMAEMA-PEO) as well as PDMAEMA-PEO without the dodecyl groups protected the denatured protein against aggregation in contrast to PDMAEMA homopolymer. No effect of the polymers on the enzymatic activity of the client protein was observed at room temperature. The polymers also partially protected the enzyme against inactivation at high temperature. The results provide a platform for creation of artificial chaperones with unfolded protein recognition which is a major feature of natural chaperones. (C) 2018 Elsevier B.V. All rights reserved.
Subject: Protein aggregation
Artificial chaperone
Protein stabilization
Thermoresponsive polymer
Protein-polyelectrolyte complexes
Poly(dimethylaminoethyl methacrylate)
INTERPOLYELECTROLYTE COMPLEXES
THERMAL AGGREGATION
PRION PROTEIN
POLYELECTROLYTE
POLYANIONS
THERMOAGGREGATION
POLYMERIZATION
DENDRIMERS
LYSOZYME
ENZYMES
116 Chemical sciences
Peer reviewed: Yes
Rights: cc_by_nc_nd
Usage restriction: openAccess
Self-archived version: acceptedVersion


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