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Issue 3, 2016
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A new concept for molecular engineering of artificial enzymes: a multiscale simulation

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Abstract

We propose a new concept for the design of artificial enzymes from synthetic protein-like copolymers and non-natural functional monomers which in terms of their affinity for water can be divided into two categories: hydrophobic and hydrophilic. Hydrophilic monomers comprise catalytically active groups similar to those in the corresponding amino acid residues. A key ingredient of our approach is that the target globular conformation of protein-like, core–shell morphology with multiple catalytic groups appears spontaneously in the course of controlled radical polymerization in a selective solvent. As a proof of concept, we construct a fully synthetic analog of serine hydrolase, e.g. α-chymotrypsin, using the conformation-dependent sequence design approach and multiscale simulation that combines the methods of “mesoscale chemistry” and atomistic molecular dynamics (MD). A 100 ns GPU-accelerated MD simulation of the designed polymer-supported catalyst in the aqueous environment provides valuable information on the structural organization of this system that has been synthesized in our Lab.

Graphical abstract: A new concept for molecular engineering of artificial enzymes: a multiscale simulation

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Publication details

The article was received on 29 Sep 2015, accepted on 27 Oct 2015 and first published on 27 Oct 2015


Article type: Paper
DOI: 10.1039/C5SM02428E
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Citation: Soft Matter, 2016,12, 689-704
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    A new concept for molecular engineering of artificial enzymes: a multiscale simulation

    P. V. Komarov, P. G. Khalatur and A. R. Khokhlov, Soft Matter, 2016, 12, 689
    DOI: 10.1039/C5SM02428E

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