Size of silk fibroin beta -sheet domains affected by Ca2

In the search for suitable scaffold materials for tissue regeneration, silk fibroin has become one of the most promising candidates due to its biocompatibility and good physical properties. To facilitate bone formation in osteochondral defects, it is often combined with a bone promoting additive. He...

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Veröffentlicht in:Journal of materials chemistry. B, Materials for biology and medicine Materials for biology and medicine, 2016-10, Vol.4 (40), p.6597-6608
Hauptverfasser: Drnovsek, N, Kocen, R, Gantar, A, Drobnic-Kosorok, M, Leonardi, A, Krizaj, I, Recnik, A, Novak, S
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container_issue 40
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container_title Journal of materials chemistry. B, Materials for biology and medicine
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creator Drnovsek, N
Kocen, R
Gantar, A
Drobnic-Kosorok, M
Leonardi, A
Krizaj, I
Recnik, A
Novak, S
description In the search for suitable scaffold materials for tissue regeneration, silk fibroin has become one of the most promising candidates due to its biocompatibility and good physical properties. To facilitate bone formation in osteochondral defects, it is often combined with a bone promoting additive. Here we demonstrate using HRTEM analysis how the release of Ca2+ ions from bioactive glass or Ca-salts results in the reduction of beta -sheet domain size that effectively controls a scaffold's properties, such as degradation and mechanical stiffness. We show that these changes already occur in silk fibroin solution prior to scaffold preparation and are caused by a decrease in zeta potential that forces fibroin molecules into tighter packing resulting in higher scaffold crystallinity, smaller beta -sheet domains and higher interconnectivity. The reduction of beta -sheet domains improves the elastic modulus and allows faster degradation despite the higher crystallinity. Ca2+ was also shown to be beneficial to the formation of hydroxy-apatite sheets on the fibroin surface.
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source Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
subjects Biocompatibility
Bones
Crystallinity
Degradation
Formations
Reduction
Scaffolds
Silk fibroin
title Size of silk fibroin beta -sheet domains affected by Ca2
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