There is no author summary for this article yet. Authors can add summaries to their articles on ScienceOpen to make them more accessible to a non-specialist audience.
Abstract
A simple chemical modification method using diazonium coupling chemistry was developed
to tailor the structure and hydrophilicity of silk fibroin protein. The extent of
modification using several aniline derivatives was characterized using UV-vis and
1H NMR spectroscopies, and the resulting protein structure was analyzed with ATR-FTIR
spectroscopy. Introduction of hydrophobic functional groups facilitated rapid conversion
of the protein from a random coil to a beta-sheet structure, while addition of hydrophilic
groups inhibited this process. hMSCs were grown on these modified silks to assess
the biocompatibility of these materials. The hydrophilicity of the silk derivatives
was found to affect the growth rate and morphology, but hMSCs were able to attach,
proliferate and differentiate into an osteogenic lineage on all of the silk derivatives.