In nature, water is vital for maintaining homeostasis. Particularly, organisms (e.g., plant leaf, bird feather) exploit water fluidics for motions. Hydration-adaptive crystallization is the representative water-responsive actuation of biopolymers. This crystallization has inspired the development of intelligent human-robot interfaces. At the same time, it hinders the consistent adhesion of tissue adhesive. As hydration-adaptive crystallization is inevitable, the on-demand control of crystallization is desirable in the innovative biopolymeric biomedical systems. To this end, this study developed an amino acid-based technology to artificially up- or down-regulate the inevitable crystallization of silk fibroin. A case II diffusion model was constructed, and it revealed that the activity of polar amino acid is related to crystallization kinetics. Furthermore, the water dynamics study suggested that active amino acid stabilizes crystallization-triggering water molecules. As a proof-of-concept, we verified that a 30% increase in the activity of serine resulted in a 50% decrease in the crystallization rate. Furthermore, the active amino acid-based suppression of hydration-adaptive crystallization enabled the silk fibroin to keep its robust adhesion (approximately 160 kJ m-3) by reducing the water-induced loss of adhesive force. The proposed silk fibroin was demonstrated as a stable tissue adhesive applied on ex vivo porcine mandible tissue. This amino acid-based regulation of hydration-adaptive crystallization will pioneer next-generation biopolymer-based healthcare.
Bibliographical notePublisher Copyright:
© 2022 American Chemical Society. All rights reserved.
All Science Journal Classification (ASJC) codes
- General Materials Science
- General Engineering
- General Physics and Astronomy