Fabrication of mechanical robust keratin adsorbent by induced molecular network transition and its dye adsorption performance

Bioinspired Robust Keratin Hydrogels for Biomedical Applications

“…To obtain robust keratin hydrogels, numerous attempts have been made by conjugating with other materials. 12,13 A strategy to mechanically improve keratin hydrogels was developed by cleaving the intramolecular disulfide bonds to generate a free thiol group that can form intermolecular disulfide bonds for strengthening. 14 As the largest subgroup of intermediate filament (IF)-forming proteins, soft keratin can self-assemble in the cells to form the IF structure and play a significant role in cells' mechanical behaviors.…”

Innovative application of magnetically modified bovine horn as a natural keratin resource in the role of value-added organocatalyst

“…As a result, benzamides that bearded electron-donating groups like methoxy and methyl (Table 2, entries 17-18) revealed more suitable results compared with electron-withdrawing groups (Table 2, entry 19). Regarding benzamide derivatives with aniline, similar to benzylamine, the presence of the electron-donating group achieved better yields compared to electron-withdrawing groups (Table 2, entries [20][21][22][23][24]. Finally, our study was focused on the transamidation of urea and thiourea with aniline and 1-phenylethylamine while corresponding target products revealed good yields (Table 2, entries [25][26][27].…”

“…However, most investigations belong to the keratin absorption capability for metals and other pollutants besides biomedical applications. [20][21][22] Resultantly, we decided to emphasize the potency of waste materials in the role of value-added products. 14,[39][40][41] Bovine horn powder (BHP) as a low-cost and abundant material could be a suitable alternative for synthetic and high-priced organocatalyst.…”

Preparation of PEG‐modified wool keratin/sodium alginate porous scaffolds with elasticity recovery and good biocompatibility

“…[20][21][22] On the other hand, the mechanical properties of regenerated keratin are poor. 23,24 This is mainly because highly active thiols after reduction are easy to combine again to form irregular aggregates, leading to unsatisfying mechanical properties, such as strong brittleness, poor elasticity, and poor strength.…”

“…On one hand, due to the existence of special peptide chains and a large number of hydrogen bonds, van der Waals forces, ionic bonds, especially disulfide bonds that are difficult to cleave, keratin is very difficult to be extracted 20‐22 . On the other hand, the mechanical properties of regenerated keratin are poor 23,24 . This is mainly because highly active thiols after reduction are easy to combine again to form irregular aggregates, leading to unsatisfying mechanical properties, such as strong brittleness, poor elasticity, and poor strength.…”