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1.
Toxicol Lett ; 386: 30-33, 2023 Sep 01.
Article in English | MEDLINE | ID: mdl-37716589

ABSTRACT

We report the successful evaluation of a US Pharmacopeia Apparatus 4 (USP-4) system in measuring the dissolution profiles of man-made vitreous fibers (MMVF)1. Glass and stone wool fibers with different (high- and low-) solubility profiles were tested in closed-loop configuration using a sodium/potassium phosphate buffer solution or an acetate buffer, respectively. Results confirm a need to operate in diluted conditions to avoid silicon saturation in the simulant solution and suppression of fiber dissolution. A clear fiber-to-fiber differentiation with good cell-to-cell reproducibility was achieved. These findings support the continued development of a USP-4 protocol for MMVF in vitro acellular testing.


Subject(s)
Glass , Humans , Animals , Solubility , Reproducibility of Results
2.
J Mater Chem B ; 4(40): 6597-6608, 2016 Oct 28.
Article in English | MEDLINE | ID: mdl-32263703

ABSTRACT

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 ß-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 ß-sheet domains and higher interconnectivity. The reduction of ß-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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