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Article

Directed Evolution and Engineering of Gallium-Binding Phage Clones—A Preliminary Study

1
Helmholtz Institute Freiberg for Resource Technology, Helmholtz-Zentrum Dresden-Rossendorf, Bautzner Landstraße 400, 01328 Dresden, Germany
2
Institute of Nonferrous Metallurgy and Purest Materials, TU Bergakademie Freiberg, Leipziger Str. 34, 09599 Freiberg, Germany
*
Author to whom correspondence should be addressed.
Biomimetics 2019, 4(2), 35; https://doi.org/10.3390/biomimetics4020035
Received: 28 February 2019 / Revised: 26 April 2019 / Accepted: 29 April 2019 / Published: 8 May 2019
(This article belongs to the Special Issue Selected Papers from N.I.C.E. 2018)
The phage surface display technology is a useful tool to screen and to extend the spectrum of metal-binding protein structures provided by nature. The directed evolution approach allows identifying specific peptide ligands for metals that are less abundant in the biosphere. Such peptides are attractive molecules in resource technology. For example, gallium-binding peptides could be applied to recover gallium from low concentrated industrial wastewater. In this study, we investigated the affinity and selectivity of five bacteriophage clones displaying different gallium-binding peptides towards gallium and arsenic in independent biosorption experiments. The displayed peptides were highly selective towards Ga3+ whereby long linear peptides showed a lower affinity and specificity than those with a more rigid structure. Cysteine scanning was performed to determine the relationship between secondary peptide structure and gallium sorption. By site-directed mutagenesis, the amino acids of a preselected peptide sequence are systematically replaced by cysteines. The resulting disulphide bridge considerably reduces the flexibility of linear peptides. Subsequent biosorption experiments carried out with the mutants obtained from cysteine scanning demonstrated, depending on the position of the cysteines in the peptide, either a considerable increase in the affinity of gallium compared to arsenic or an increase in the affinity for arsenic compared to gallium. This study shows the impressive effect on peptide–target interaction based on peptide structure and amino acid position and composition via the newly established systematic cysteine scanning approach. View Full-Text
Keywords: phage surface display; gallium; metal–peptide interaction; site-directed mutagenesis; cysteine; peptide structure phage surface display; gallium; metal–peptide interaction; site-directed mutagenesis; cysteine; peptide structure
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MDPI and ACS Style

Schönberger, N.; Zeitler, C.; Braun, R.; Lederer, F.L.; Matys, S.; Pollmann, K. Directed Evolution and Engineering of Gallium-Binding Phage Clones—A Preliminary Study. Biomimetics 2019, 4, 35. https://doi.org/10.3390/biomimetics4020035

AMA Style

Schönberger N, Zeitler C, Braun R, Lederer FL, Matys S, Pollmann K. Directed Evolution and Engineering of Gallium-Binding Phage Clones—A Preliminary Study. Biomimetics. 2019; 4(2):35. https://doi.org/10.3390/biomimetics4020035

Chicago/Turabian Style

Schönberger, Nora, Christina Zeitler, Robert Braun, Franziska L. Lederer, Sabine Matys, and Katrin Pollmann. 2019. "Directed Evolution and Engineering of Gallium-Binding Phage Clones—A Preliminary Study" Biomimetics 4, no. 2: 35. https://doi.org/10.3390/biomimetics4020035

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