Molecular crowding facilitates assembly of spidroin-like proteins through phase separation
| Autor: | Laura Lemetti, Heikki Tenhu, Piotr Batys, Dmitrii Fedorov, A. Sesilja Aranko, Sami-Pekka Hirvonen, Markus Linder, Maria Sammalkorpi |
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| Přispěvatelé: | Department of Bioproducts and Biosystems, University of Helsinki, Department of Chemistry and Materials Science, Aalto-yliopisto, Aalto University, Department of Chemistry, Polymers |
| Rok vydání: | 2019 |
| Předmět: |
Biopolymer
Polymers and Plastics 116 Chemical sciences General Physics and Astronomy CONFINEMENT 02 engineering and technology engineering.material 010402 general chemistry 01 natural sciences Molecular crowding DEXTRAN Spidroin SILKS Materials Chemistry Molecule Spider silk Fiber Self-coacervation Coacervate Chemistry Organic Chemistry ta1182 Coacervation Isothermal titration calorimetry 021001 nanoscience & nanotechnology Fusion protein 0104 chemical sciences Liquid-liquid phase separation FRAP Biophysics engineering ADHESIVE 0210 nano-technology BEHAVIOR |
| Zdroj: | European Polymer Journal. 112:539-546 |
| ISSN: | 0014-3057 |
| Popis: | Gaining insights into the processes that transform dispersed biopolymers into well-ordered structures, such as soluble spidroin-proteins to spider silk threads, is essential for attempts to understand their biological function and to mimic their unique properties. One of these processes is liquid-liquid phase separation, which can act as an intermediate step for molecular assembly. We have shown that a self-coacervation step that occurs at a very high protein concentration (> 200 gl(-1)) is crucial for the fiber assembly of an engineered triblock silk-like molecule. In this study, we demonstrate that the addition of a crowding agent lowers the concentration at which coacervation occurs by almost two orders of magnitude. Coacervates induced by addition of a crowding agent are functional in terms of fiber formation, and the crowding agent appears to affect the process solely by increasing the effective concentration of the protein. Furthermore, induction at lower concentrations allows us to study the thermodynamics of the system, which provides insights into the coacervation mechanism. We suggest that this approach will be valuable for studies of biological coacervating systems in general. |
| Databáze: | OpenAIRE |
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