Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting SARS-CoV-2

Hristo L. Svilenov; Florent Delhommel; Till Siebenmorgen; Florian Rührnößl; Grzegorz M. Popowicz; Alwin Reiter; Michael Sattler; Carsten Brockmeyer; Johannes Buchner

doi:10.1038/s42003-023-04762-w

Communications Biology (Apr 2023)

Extrinsic stabilization of antiviral ACE2-Fc fusion proteins targeting SARS-CoV-2

Hristo L. Svilenov,
Florent Delhommel,
Till Siebenmorgen,
Florian Rührnößl,
Grzegorz M. Popowicz,
Alwin Reiter,
Michael Sattler,
Carsten Brockmeyer,
Johannes Buchner

Affiliations

Hristo L. Svilenov: Center for Functional Protein Assemblies (CPA) and School of Natural Sciences, Department of Bioscience, Technical University of Munich
Florent Delhommel: Institute of Structural Biology, Helmholtz Zentrum München
Till Siebenmorgen: Institute of Structural Biology, Helmholtz Zentrum München
Florian Rührnößl: Center for Functional Protein Assemblies (CPA) and School of Natural Sciences, Department of Bioscience, Technical University of Munich
Grzegorz M. Popowicz: Institute of Structural Biology, Helmholtz Zentrum München
Alwin Reiter: Formycon AG
Michael Sattler: Institute of Structural Biology, Helmholtz Zentrum München
Carsten Brockmeyer: Brockmeyer Biopharma GmbH
Johannes Buchner: Center for Functional Protein Assemblies (CPA) and School of Natural Sciences, Department of Bioscience, Technical University of Munich

DOI: https://doi.org/10.1038/s42003-023-04762-w
Journal volume & issue: Vol. 6, no. 1
pp. 1 – 9

Abstract

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The solution structure, stability, and dynamics of a broadly-acting antiviral ACE2-IgG-Fc fusion protein are determined. Small chemical compounds binding to ACE2 can be used to drastically increase the thermal stability of the ACE2 domain.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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