Modification of silk fibroin using diazonium coupling chemistry and the effects on hMSC proliferation and differentiation.

Biomaterials
Amanda R MurphyDavid L Kaplan

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.

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Citations

Jan 17, 2013·ACS Applied Materials & Interfaces·Isabella S RomeroAmanda R Murphy
Nov 26, 2010·Biomacromolecules·Sejuti SenguptaDavid L Kaplan
Nov 5, 2011·Biomacromolecules·Chunhong YeVladimir V Tsukruk
Sep 13, 2012·Biomacromolecules·Soumen DasSayam Sen Gupta
Feb 7, 2013·Journal of the American Chemical Society·Zhongyuan SunDavid L Kaplan
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Oct 1, 2011·Nature Protocols·Danielle N RockwoodDavid L Kaplan
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Mar 22, 2014·ACS Applied Materials & Interfaces·Vartika Dhyani, Neetu Singh
Sep 22, 2015·Advanced Materials·Eunhee JeoungVincent M Rotello
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Jul 25, 2012·Biomaterials·Rossella Calabrese, David L Kaplan
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Aug 13, 2013·Acta Biomaterialia·F Raquel MaiaCristina C Barrias
Apr 22, 2015·Biomacromolecules·Paige N AtterberryAmanda R Murphy

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