Abstract
Silk fibroin-derived polypeptides (FDPs) are polypeptides resulting from the enzymatic separation of the hydrophobic crystalline (Cp) and hydrophilic electronegative amorphous (Cs) components of silk fibroin (SF). The role of these polypeptides in promoting the nucleation of hydroxyapatite (HA) has been previously investigated, yet is still not fully understood. Here we study the potential of HA mineralization via FDPs incorporated at 1:10, 1:2 and 1:1 in a plastically compressed (PC) and dense collagen (DC) scaffold. Scaffolds were immersed in simulated body fluid (SBF) at physiological conditions (pH = 7.4, 37°C) to promote biomineralization. The effect of Cs and Cp to promote HA nucleation was investigated at different time points, and compared to pure DC scaffolds. Characterization of Cs and Cp fragments using Liquid Chromatography-Mass Spectrometry (LCMS) showed little difference in the amino acid composition of the FDPs. Results obtained in vitro using Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy (ATR-FTIR), Scanning Electron Microscopy (SEM) X-Ray Diffraction (XRD) and mass analysis showed little difference between scaffolds that incorporated Cs, Cp, and DC hydrogels. These results demonstrated that silk FDPs incorporation are not yet suitable to promote HA nucleation in vivo without further refining the collagen-FDP system.