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

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.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Semenyuk P,Tiainen T,Hietala S,Tenhu H,Aseyev V,Muronetz V

doi

10.1016/j.ijbiomac.2018.10.031

subject

Has Abstract

pub_date

2019-01-01 00:00:00

pages

536-545

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(18)33873-X

journal_volume

121

pub_type

杂志文章

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