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DOI: 10.1055/a-2219-6830
Catalytically Competent Fluorinated Barnase Variants
Financial support for this work was provided by the Deutsche Forschungsgemeinschaft (DFG) through the SFB 1349 Fluor-Spezifische Wechselwirkungen and the graduate school IMPRS (International Max-Planck Research School) on Multiscale Biosystems of the Max-Planck Institute for Colloids and Interfaces.
Abstract
Proteins play critical roles in all living organisms, and their properties and functions result directly from their primary sequences. Fluorine, though seldom found in natural organic compounds, has been shown to impart desirable properties to small molecules and proteins alike. However, studies on the impact of this element in enzyme activity and protein–protein interaction are largely absent from the literature. Here we present a microwave-assisted SPPS method for the total synthesis of site-specifically fluorinated barnase variants, as well as characterization of their folding and activity. CD spectroscopy and fluorescence-based activity assays show that the fluorinated amino acids are generally not perturbative of the protein structure and that enzyme activity, albeit reduced, is retained in all variants.
Supporting Information
- Supporting information for this article is available online at https://doi.org/10.1055/a-2219-6830.
- Supporting Information
Publication History
Received: 05 October 2023
Accepted after revision: 29 November 2023
Accepted Manuscript online:
29 November 2023
Article published online:
05 February 2024
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