Hydration-Induced Structural Transitions in Biomimetic Tandem Repeat Proteins
| Autor: | Huihun Jung, Melik C. Demirel, Chloe H. Skidmore, Romeo C. A. Dubini, Petra Rovó |
|---|---|
| Rok vydání: | 2021 |
| Předmět: |
Toughness
Magnetic Resonance Spectroscopy Materials science Proline 010304 chemical physics Rational design Proteins Conductivity 010402 general chemistry 01 natural sciences Microscopic scale 0104 chemical sciences Surfaces Coatings and Films Amorphous solid Characterization (materials science) Biomimetics Tandem Repeat Sequences Chemical physics 0103 physical sciences Materials Chemistry Physical and Theoretical Chemistry Elasticity (economics) Isomerization |
| Zdroj: | The Journal of Physical Chemistry B. 125:2134-2145 |
| ISSN: | 1520-5207 1520-6106 |
| Popis: | A major challenge in developing biomimetic, high-performance, and sustainable products is the accurate replication of the biological materials' striking properties, such as high strength, self-repair, and stimuli-responsiveness. The rationalization of such features on the microscopic scale, together with the rational design of synthetic materials, is currently hindered by our limited understanding of the sequence-structure-property relationship. Here, employing state-of-the-art nuclear magnetic resonance (NMR) spectroscopy, we link the atomistic structural and dynamic properties of an artificial bioinspired tandem repeat protein TR(1,11) to its stunning macroscopic properties including high elasticity, self-healing capabilities, and record-holding proton conductivity among biological materials. We show that the hydration-induced structural rearrangement of the amorphous Gly-rich soft segment and the ordered Ala-rich hard segment is the key to the material's outstanding physical properties. We found that in the hydrated state both the Ala-rich ordered and Gly-rich disordered parts contribute to the formation of the nanoconfined β-sheets, thereby enhancing the strength and toughness of the material. This restructuring is accompanied by fast proline ring puckering and backbone cis-trans isomerization at the water-protein interface, which in turn enhances the elasticity and the thermal conductivity of the hydrated films. Our in-depth characterization provides a solid ground for the development of next-generation materials with improved properties. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|