Rational Design of Supramolecular Dynamic Protein Assemblies by Using a Micelle-Assisted Activity-Based Protein-Labeling Technology
| Autor: | Sugam Kumar, Britto S. Sandanaraj, Pavankumar Janardhan Bhandari, Mullapudi Mohan Reddy, Vinod K. Aswal |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Light Macromolecular Substances Protein Conformation Surface Properties Supramolecular chemistry Nanotechnology Protein Engineering 010402 general chemistry 01 natural sciences Micelle Catalysis Hydrophobic effect 03 medical and health sciences Amphiphile Trypsin Micelles Bioconjugation Chemistry Organic Chemistry Rational design Proteins General Chemistry Protein engineering Hydrogen-Ion Concentration Photochemical Processes 0104 chemical sciences Kinetics 030104 developmental biology Protein Multimerization Serine Proteases Hydrophobic and Hydrophilic Interactions Macromolecule |
| Zdroj: | Chemistry - A European Journal. 24:16085-16096 |
| ISSN: | 0947-6539 |
| DOI: | 10.1002/chem.201802824 |
| Popis: | The self-assembly of proteins into higher-order superstructures is ubiquitous in biological systems. Genetic methods comprising both computational and rational design strategies are emerging as powerful methods for the design of synthetic protein complexes with high accuracy and fidelity. Although useful, most of the reported protein complexes lack a dynamic behavior, which may limit their potential applications. On the contrary, protein engineering by using chemical strategies offers excellent possibilities for the design of protein complexes with stimuli-responsive functions and adaptive behavior. However, designs based on chemical strategies are not accurate and therefore, yield polydisperse samples that are difficult to characterize. Here, we describe simple design principles for the construction of protein complexes through a supramolecular chemical strategy. A micelle-assisted activity-based protein-labeling technology has been developed to synthesize libraries of facially amphiphilic synthetic proteins, which self-assemble to form protein complexes through hydrophobic interaction. The proposed methodology is amenable for the synthesis of protein complex libraries with molecular weights and dimensions comparable to naturally occurring protein cages. The designed protein complexes display a rich structural diversity, oligomeric states, sizes, and surface charges that can be engineered through the macromolecular design. The broad utility of this method is demonstrated by the design of most sophisticated stimuli-responsive systems that can be programmed to assemble/disassemble in a reversible/irreversible fashion by using the pH or light as trigger. |
| Databáze: | OpenAIRE |
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