Hydration-Induced Structural Transitions in Biomimetic Tandem Repeat Proteins

Area of Science:

• Biomaterials Science
• Protein Engineering
• Spectroscopy

Background:

• Replicating biological material properties (strength, self-repair, stimuli-responsiveness) in synthetic materials is challenging.
• Limited understanding of sequence-structure-property relationships hinders biomimetic material design.
• Artificial proteins offer a platform for developing advanced biomaterials.

Purpose of the Study:

• To elucidate the atomistic structure-dynamics-property relationships of an artificial bioinspired protein, TR(1,11).
• To correlate microscopic features with macroscopic properties like elasticity, self-healing, and proton conductivity.
• To provide a foundation for designing next-generation high-performance biomaterials.

Main Methods:

• Utilized state-of-the-art nuclear magnetic resonance (NMR) spectroscopy.
• Investigated atomistic structural and dynamic properties of the TR(1,11) protein.
• Analyzed hydration-induced structural rearrangements and their impact on material properties.

Main Results:

• Linked NMR-derived properties of TR(1,11) to its high elasticity, self-healing, and record proton conductivity.
• Identified hydration-induced rearrangement of Gly-rich (amorphous) and Ala-rich (ordered) segments as key.
• Observed nanoconfined β-sheet formation in hydrated states, enhancing strength and toughness.
• Found water-protein interface dynamics (proline puckering, cis-trans isomerization) enhance elasticity and thermal conductivity.

Conclusions:

• Hydration-induced structural and dynamic changes in TR(1,11) are critical for its superior macroscopic properties.
• The study provides fundamental insights into sequence-structure-property correlations in biomimetic materials.
• This work paves the way for designing advanced synthetic materials inspired by nature.