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A bio-inspired multifunctionalized silk fibroin (BMS) was synthesized in order to mimic the interaction of nidogen with the type IV collagen and laminin of basement membranes. The designed BMS consists of a motif of laminin α-chain-derived, called IK peptide, and type IV collagen covalently bound to the silk fibroin (SF) by using EDC/NHS coupling and a Cu-free click chemistry reaction, respectively. Silk fibroin was chosen as the main component of the BMS because it is versatile and biocompatible, induces an in vivo favorable bioresponse, and moreover can be functionalized with different methods. The chemical structure of BMS was analyzed by using X-ray photoelectron spectroscopy, attenuated total reflection-Fourier transform infrared, cross-polarization magic angle spinning nuclear magnetic resonance techniques, and colorimetric assay. The SF and BMS solutions were cross-linked by sonication to form hydrogels or casted to make films in order to evaluate and compare the early adhesion and viability of MRC5 cells. BMS hydrogels were also characterized by rheological and thermal analyses.

Citation

Sofia Santi, Ines Mancini, Sandra Dirè, Emanuela Callone, Giorgio Speranza, Nicola Pugno, Claudio Migliaresi, Antonella Motta. A Bio-inspired Multifunctionalized Silk Fibroin. ACS biomaterials science & engineering. 2021 Feb 08;7(2):507-516

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PMID: 33476122

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