Details
| Original language | English |
|---|---|
| Pages (from-to) | 12240-12245 |
| Number of pages | 6 |
| Journal | Journal of the American Chemical Society |
| Volume | 141 |
| Issue number | 31 |
| Publication status | Published - 7 Aug 2019 |
| Externally published | Yes |
Abstract
Proteins controlling mineralization in vivo are diverse, suggesting that there are various ways by which mineralization can be directed in bioinspired approaches. While well-defined three-dimensional (3D) structures occur in biomineralization proteins, the design of synthetic, soluble, bioinspired macromolecules with specific, reproducible, and predictable 3D arrangements of mineral-interacting functions poses an ultimate challenge. Thus, the question of how certain arrangements of such functions on protein surfaces influence mineralization and in what ways specific alterations subsequently affect this process remains elusive. Here we used genetically engineered ubiquitin (Ub) proteins in order to overcome the limitations of generic bioinspired additive systems. By advancing existing protocols, we introduced an unnatural amino acid and subsequently mineral-interacting functions via selective-pressure incorporation and click chemistry, respectively, without affecting the Ub secondary structure. Indeed, as-obtained Ub with three phosphate functions at defined positions shows unique effects based on a yet-unmatched capability toward the stabilization of a film of a dense liquid mineral phase visible even with the naked eye and its transformation into amorphous nanoparticles and afterward crystals with complex shapes. We thereby demonstrate that Ub designer proteins pose a unique new generation of crystallization additives where the 3D arrangement of mineral-interacting functions can be designed at will, promising their future use for programmable, target-oriented mineralization control.
ASJC Scopus subject areas
- Chemical Engineering(all)
- Catalysis
- Chemistry(all)
- General Chemistry
- Biochemistry, Genetics and Molecular Biology(all)
- Biochemistry
- Chemical Engineering(all)
- Colloid and Surface Chemistry
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In: Journal of the American Chemical Society, Vol. 141, No. 31, 07.08.2019, p. 12240-12245.
Research output: Contribution to journal › Article › Research › peer review
}
TY - JOUR
T1 - Ubiquitin Designer Proteins as a New Additive Generation toward Controlling Crystallization
AU - Ruiz-Agudo, Cristina
AU - Lutz, Joachim
AU - Keckeis, Philipp
AU - King, Michael
AU - Marx, Andreas
AU - Gebauer, Denis
N1 - Funding Information: This work was performed within the framework of SFB 1214 (Project A07) funded by the German Research Foundation (DFG). D.G. was a Research Fellow of the Zukunftskolleg of the University of Konstanz during this work. C.R.-A. thanks SFB 1214 and the Zukunftskolleg of the University of Konstanz for financial support. We thank the personnel of the Centro de Instrumentación Científica (University of Granada) for their support and help with the ESEM, FESEM, and TEM analyses. In addition, we thank the Particle Analysis Center of the University of Konstanz (funded by SFB 1214). We also thank Prof. Dr. Christine Peter for comments that greatly improved the manuscript.
PY - 2019/8/7
Y1 - 2019/8/7
N2 - Proteins controlling mineralization in vivo are diverse, suggesting that there are various ways by which mineralization can be directed in bioinspired approaches. While well-defined three-dimensional (3D) structures occur in biomineralization proteins, the design of synthetic, soluble, bioinspired macromolecules with specific, reproducible, and predictable 3D arrangements of mineral-interacting functions poses an ultimate challenge. Thus, the question of how certain arrangements of such functions on protein surfaces influence mineralization and in what ways specific alterations subsequently affect this process remains elusive. Here we used genetically engineered ubiquitin (Ub) proteins in order to overcome the limitations of generic bioinspired additive systems. By advancing existing protocols, we introduced an unnatural amino acid and subsequently mineral-interacting functions via selective-pressure incorporation and click chemistry, respectively, without affecting the Ub secondary structure. Indeed, as-obtained Ub with three phosphate functions at defined positions shows unique effects based on a yet-unmatched capability toward the stabilization of a film of a dense liquid mineral phase visible even with the naked eye and its transformation into amorphous nanoparticles and afterward crystals with complex shapes. We thereby demonstrate that Ub designer proteins pose a unique new generation of crystallization additives where the 3D arrangement of mineral-interacting functions can be designed at will, promising their future use for programmable, target-oriented mineralization control.
AB - Proteins controlling mineralization in vivo are diverse, suggesting that there are various ways by which mineralization can be directed in bioinspired approaches. While well-defined three-dimensional (3D) structures occur in biomineralization proteins, the design of synthetic, soluble, bioinspired macromolecules with specific, reproducible, and predictable 3D arrangements of mineral-interacting functions poses an ultimate challenge. Thus, the question of how certain arrangements of such functions on protein surfaces influence mineralization and in what ways specific alterations subsequently affect this process remains elusive. Here we used genetically engineered ubiquitin (Ub) proteins in order to overcome the limitations of generic bioinspired additive systems. By advancing existing protocols, we introduced an unnatural amino acid and subsequently mineral-interacting functions via selective-pressure incorporation and click chemistry, respectively, without affecting the Ub secondary structure. Indeed, as-obtained Ub with three phosphate functions at defined positions shows unique effects based on a yet-unmatched capability toward the stabilization of a film of a dense liquid mineral phase visible even with the naked eye and its transformation into amorphous nanoparticles and afterward crystals with complex shapes. We thereby demonstrate that Ub designer proteins pose a unique new generation of crystallization additives where the 3D arrangement of mineral-interacting functions can be designed at will, promising their future use for programmable, target-oriented mineralization control.
UR - http://www.scopus.com/inward/record.url?scp=85070540715&partnerID=8YFLogxK
U2 - 10.1021/jacs.9b06473
DO - 10.1021/jacs.9b06473
M3 - Article
VL - 141
SP - 12240
EP - 12245
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 31
ER -