This novel conjugation strategy utilizes a polyethylene oxide (PEO) cylindrical molecular brush architecture to design a self-assembled structure for thermal stabilization of enzymes. The moderately stiff polymer ligand structure originates from side PEO chains grafted to the polymer backbone that carries reactive epoxy functional groups. The molecular brush is bound via epoxy functional groups to lysine’s amino groups on the surface of the enzyme globule, promoting the formation of stiff and crowded cages around the enzymes and preventing the water molecules access to the enzyme and enzymes agglomeration. The excluded volume effect introduced by the densely grafted PEO chains results in a significant improvement of biocatalytic activity and thermal stability of lysozyme and trypsin that retain their activity even upon heating to 100<sup>o</sup>C and above. The molecular dynamic simulations show that the high concentration of polyethylene oxide in the vicinity of the enzyme is critical for their thermal stability At high temperatures, a number of hydrogen bonds remains high and corresponding conformational changes in the protein remains low, indicating a high degree of resilience of the secondary structure and thereby contributing to the high rates of the residual activity.

Thermal stabilization of enzymes with biocompatible stiff polymer brush ligands

255th National Meeting (2018)

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