Fabrication and characterization of novel diopside/silk fibroin nanocomposite scaffolds for potential application in maxillofacial bone regeneration

Doped Calcium Silicate Ceramics: A New Class of Candidates for Synthetic Bone Substitutes

“…Nano-sized diopside powder incorporated at 20–40 wt % into a silk fibroin matrix resulted in decreased porosity, increased compressive strength (~0.1 MPa to ~0.4 MPa) and modulus (~1 MPa to ~4 MPa), and slightly improved proliferation of MC3T3-E1 cells [125]. Diopside particles incorporated into a chitosan matrix were found to reduce the water retention capacity of the composite, while promoting the expression of osteogenic markers (ALP and collagen type I) in MG-63 cells [126].…”

Silk as a potential candidate for bone tissue engineering

“…It can induce β-sheet conformation without the need for other hazardous solvents such as methanol [173]. Generally speaking, it seems that incorporation of ceramic components into SF matrices can not only improve the mechanical properties of silk scaffolds but also enhance their biocompatibility.…”

Preparation, characterization, degradation and biocompatibility of different silk fibroin based composite scaffolds prepared by freeze-drying method for tissue engineering application

“…The amino acid composition of fibroin consists of glycine, alanine, and serine, forming β-sheets in the form of an anti-parallel in spun fibers that can provide good mechanical strength [1,3]. Silk fibroin has been widely investigated as a biomaterial and scaffold for different types of tissue engineering applications because of its favorable properties such as slow biodegradation, good biocompatibility, high tensile strength, M A N U S C R I P T A C C E P T E D ACCEPTED MANUSCRIPT 3 non-cytotoxicity, low immunogenicity, controllable biodegradability, non-inflammatory and adjustable mechanical and biochemical features [15,16].…”

“…The absorption bands at 1520 cm −1 (amide II) and 1226 cm −1 (amide III) corresponded to the silk I conformation (random coil and α-helix)(Fig. 2a)[16]. The FT-IR spectra of gelatin indicated peaks at 3423 cm -1 and 3174 cm -1 due to -NH stretching of the secondary amide, C-H stretching at 2922 cm -1 and 2850 cmthe space of amino acid molecule such as aspartic acid (ASP) in SF, nHAp particles could grow longer in this direction.…”