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Article Dans Une Revue Chemistry - A European Journal Année : 2017

αRep A3: A versatile artificial scaffold for metalloenzyme design

Résumé

αRep is a new family of artificial proteins based on a thermostable alpha-helical repeated motif. One of its members, αRep A3, forms a stable homo-dimer with a wide cleft that is able to receive metal complexes and thus appears as suitable for generating new artificial biocatalysts. Based on the crystal structure of αRep A3, two positions (F119 and Y26) were chosen and changed independently into cysteine residues. A phenanthroline ligand was covalently attached to the unique cysteine of each protein variant and the corresponding biohybrids were purified and characterized. Once mutated and coupled to phenanthroline, the protein remained folded and dimeric. Copper(II) was bound specifically by the two biohybrids with two different binding modes and, in addition, the holo biohybrid A3F119NPH was found to be able to catalyze enantioselectively the Diels-Alder (D-A) cycloaddition with up to 62% ee. This study validates the choice of the αRep A3 dimer as a protein scaffold and provides a new promising route for the design and production of new enantioselective biohybrids based on entirely artificial proteins issued from a highly diverse library.
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Dates et versions

hal-02191704 , version 1 (23-07-2019)

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Thibault Di Meo, Wadih Ghattas, Christian Herrero, Christophe Velours, Philippe Minard, et al.. αRep A3: A versatile artificial scaffold for metalloenzyme design. Chemistry - A European Journal, 2017, ⟨10.1002/chem.201701518⟩. ⟨hal-02191704⟩
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