Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

Silicification and biosilicification: Part 5 - An investigation of the silica structures formed at weakly acidic pH and neutral pH as facilitated by cationically charged macromolecules

Patwardhan, S V and Clarson, S J (2003) Silicification and biosilicification: Part 5 - An investigation of the silica structures formed at weakly acidic pH and neutral pH as facilitated by cationically charged macromolecules. Journal of Materials Science, 23 (4). pp. 495-499. ISSN 0022-2461

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

Biosilicification in diatoms has been reported to occur at (or close to) neutral pH and it has been shown that protein molecules can act as catalysts/templates/scaffolds for this elegant materials chemistry. Here we report the formation of silica spheres from an aqueous silica precursor as facilitated by both poly-L-lysine (PLL) and poly(allylamine hydrochloride) (PAH) at pH 6.0 and under ambient conditions. It was observed by scanning electron microscopy (SEM) that there were morphological differences in the silica formed at pH 6 when compared to the silica morphologies formed using the same macromolecules at neutral pH. Notably, a bimodal distribution of silica particles was seen ford both the PLL and PAH systems at pH 6. These results are compared and contrasted with those previously reported for the pH dependence of silicification and biosilicification and in particular, those obtained for the pH dependence of silica formation in the presence silaffin proteins isolated form the diatom C fusiformis. The findings for these cationically charged macromolecules suggest that lysine may be an important amino acid in the primary sequence of proteins that catalyze the formation of silica structures in vivo. (C) 2002 Elsevier Science B.V. All rights reserved.