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Folding and Characterization of a Bio-responsive Robot from DNA Origami

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Building proficient enzymes with foldamer prostheses.

Clemens Mayer¹, Manuel M Müller, Samuel H Gellman

¹Laboratory of Organic Chemistry, ETH Zürich, Hönggerberg HCI F339, 8093 Zürich (Switzerland).

Angewandte Chemie (International Ed. in English)

|May 16, 2014

Summary

Researchers created novel semisynthetic enzymes using foldamer subunits for catalysis. These hybrid catalysts, built from alpha- and beta-amino acids, show high proficiency, expanding enzyme engineering possibilities with non-natural backbones.

Keywords:

enzymes foldamers protein design protein engineering β-amino acids

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Area of Science:

Biochemistry
Synthetic Biology
Catalysis

Background:

Foldamers are synthetic oligomers mimicking protein structures.
Developing novel catalysts is crucial for various scientific applications.

Purpose of the Study:

To assess the catalytic potential of foldameric subunits.
To design and characterize semisynthetic enzymes incorporating foldamer fragments.

Main Methods:

Constructing semisynthetic enzymes using α- and β-amino acid residues.
Systematically varying the α→β substitution pattern.
Evaluating the catalytic proficiency of the designed hybrid catalysts.

Main Results:

Achieved highly proficient hybrid catalysts through foldamer incorporation.
Demonstrated successful integration of non-natural backbones into enzyme engineering.
Identified optimal α→β substitution patterns and β-residue types for enhanced catalysis.

Conclusions:

Foldameric subunits are feasible for creating advanced catalytic systems.
Semisynthetic enzymes with non-natural backbones offer a promising avenue for enzyme engineering.
This work expands the toolkit for designing bespoke biocatalysts.