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Adv Mater. 2020 Jan 15:e1905309. doi: 10.1002/adma.201905309. [Epub ahead of print]

Supercharged Proteins and Polypeptides.

Author information

1
Zernike Institute for Advanced Materials, Nijenborgh 4, 9747 AG, Groningen, The Netherlands.
2
DWI - Leibniz Institute for Interactive Materials, Forckenbeckstr. 50, 52056, Aachen, Germany.
3
State Key Laboratory of Rare Earth Resource Utilization, Changchun Institute of Applied Chemistry, Chinese Academy of Sciences, 130022, Changchun, China.
4
Institute of Technical and Macromolecular Chemistry, RWTH Aachen University, Worringerweg 2, 52074, Aachen, Germany.

Abstract

Electrostatic interactions play a vital role in nature. Biomacromolecules such as proteins are orchestrated by electrostatics, among other intermolecular forces, to assemble and organize biochemistry. Natural proteins with a high net charge exist in a folded state or are unstructured and can be an inspiration for scientists to artificially supercharge other protein entities. Recent findings show that supercharging proteins allows for control of their properties such as temperature resistance and catalytic activity. One elegant method to transfer the favorable properties of supercharged proteins to other proteins is the fabrication of fusions. Genetically engineered, supercharged unstructured polypeptides (SUPs) are just one promising fusion tool. SUPs can also be complexed with artificial entities to yield thermotropic and lyotropic liquid crystals and liquids. These architectures represent novel bulk materials that are sensitive to external stimuli. Interestingly, SUPs undergo fluid-fluid phase separation to form coacervates. These coacervates can even be directly generated in living cells or can be combined with dissipative fiber assemblies that induce life-like features. Supercharged proteins and SUPs are developed into exciting classes of materials. Their synthesis, structures, and properties are summarized. Moreover, potential applications are highlighted and challenges are discussed.

KEYWORDS:

adaptive soft matter; electrostatic interactions; functional assembly; supercharged proteins; supercharged unstructured polypeptides

PMID:
31943419
DOI:
10.1002/adma.201905309

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