α-chymotrypsin activated and stabilized by self-assembled polypseudorotaxane fabricated with bis-thiolated poly(ethylene glycol) and α-cyclodextrin: Spectroscopic and mechanistic analysis.
作者： Jun Zhao , Ji-Duan Lin , Jia-Chen Chen , Guo Chen , Xia-Lan Li
DOI: 10.1016/J.IJBIOMAC.2017.05.024
关键词:
摘要: Abstract The self-assembled polypseudorotaxane (PPRX) fabricated with bis-thiolated poly(ethylene glycol) (PEG) and α-cyclodextrin (α-CyD) acted as an activator for α-chymotrypsin (CT) retained the activity of CT a long time up to 7 days. stabilization mechanism was studied, interaction between PPRX analyzed by using circular dichroism, fluorescence spectra X-ray powder diffraction (XRD). PEG its assembled α-CyD exhibited C -terminal region CT’s B-chain probably through PEGylation surface disulfide bridge CT. It caused aromatic chromophores more exposed hydrophilic microenvironment, leading conformational variation that revealed spectroscopic analysis. rendered peptide chains in flexible active state. As comparison, non-thiolated components could not decorate performed almost no effect on stability, which demonstrated decoration key factor retaining Due activation effect, PEG/α-CyD excellent soft-immobilized carrier CT, provided intriguing method enzyme’s stabilization.
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