Chemical unfolding of protein domains induces shape change in programmed protein hydrogels

• Published in: Nature communications Vol. 10; no. 1; pp. 5439 - 9
• Main Authors: Khoury, Luai R., Popa, Ionel
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 29.11.2019; Nature Publishing Group; Nature Portfolio
• Subjects: 147/135; 631/57; 639/166/985; 639/301/357; 639/301/54; Animals; Biocompatible Materials; Biomaterials; Biomechanical Phenomena; Biomechanics; Biomedical materials; Bovine serum albumin; Cattle; Composite materials; Elasticity; Humanities and Social Sciences; Hydrogels; Hydrogels - chemistry; Hydrogels - metabolism; Lysine; multidisciplinary; Nanostructures; Organic chemistry; Poly-L-lysine; Polyelectrolytes; Polyethyleneimine; Polyethyleneimine - metabolism; Polylysine - metabolism; Polymers; Protein engineering; Protein folding; Protein Unfolding; Proteins; Science; Science (multidisciplinary); Serum albumin; Serum Albumin, Bovine - chemistry; Serum Albumin, Bovine - metabolism; Shape memory; Stiffness

Programmable behavior combined with tailored stiffness and tunable biomechanical response are key requirements for developing successful materials. However, these properties are still an elusive goal for protein-based biomaterials. Here, we use protein-polymer interactions to manipulate the stiffnes...