a
Institute of Chemistry and Biochemistry, Freie Universität Berlin, Arnimallee 20 14195 Berlin, Germany
,
Michael Krummhaar
b
Max Planck Institute of Colloids and Interfaces, Arnimallee 22 14195 Berlin, Germany
,
Christian Roth
b
Max Planck Institute of Colloids and Interfaces, Arnimallee 22 14195 Berlin, Germany
,
Beate Koksch∗
a
Institute of Chemistry and Biochemistry, Freie Universität Berlin, Arnimallee 20 14195 Berlin, Germany
› Author Affiliations 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.
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.
Key words
protein synthesis -
fluorinated amino acids -
enzyme activity
Supporting Information
Supporting information for this article is available online at https://doi.org/10.1055/a-2219-6830.
3
Newberry RW,
Raines RT.
4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding
of Peptides and Proteins. In
Peptidomimetics I
.
Lubell WD.
Springer International Publishing; Cham: 2017: 1-25
