| Autor: |
Heichel DL; Polymer Program, Institute of Materials Science, University of Connecticut, 97 North Eagleville Road Unit 3136, Storrs, Connecticut 06269-3136, United States., Burke KA; Polymer Program, Institute of Materials Science, University of Connecticut, 97 North Eagleville Road Unit 3136, Storrs, Connecticut 06269-3136, United States.; Department of Chemical and Biomolecular Engineering, University of Connecticut, 191 Auditorium Road Unit 3222, Storrs, Connecticut 06269-3222, United States.; Department of Biomedical Engineering, University of Connecticut, 260 Glenbrook Road Unit 3247, Storrs, Connecticut 06269-3247, United States. |
| Abstrakt: |
Silk fibroin is a semicrystalline protein used as a renewable polymer source and as a biomaterial platform, but existing methods to synthetically modify fibroin suffer from low efficiencies that can limit the protein's utility. This work reports on a mild synthesis that results in a 2-fold increase in carboxylation through the disruption of noncovalent interactions during the reaction. Importantly, silk fibroin maintains its ability to form β-sheets that are critical for tailoring mechanical and degradation properties, as well as for rendering solid constructs (e.g., films and scaffolds) insoluble in water. Increasing carboxyl functionalization affords control over protein charge, which permits tailoring the loading and release of small molecules using electrostatic interactions. Disruption of noncovalent interactions during aqueous carbodiimide coupling also significantly enhances conjugation efficiency of molecules containing primary amine groups, thus enabling high degrees of functionalization with biological molecules, such as proteins and peptides, for biomaterial applications. |
