Possible model of protein nucleation and crystallization on porous silicon
β Scribed by Stolyarova, S. ;Baskin, E. ;Chayen, N. E. ;Nemirovsky, Y.
- Book ID
- 105363136
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 68 KB
- Volume
- 202
- Category
- Article
- ISSN
- 0031-8965
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β¦ Synopsis
Abstract
The problem of macromolecular nucleation and crystallization on porous silicon surface is investigated theoretically. The fractality of the porous silicon layer is exploited. It is shown that the effective surface density of adsorbed particles on a fractal selfβsimilar surface significantly exceeds that on a flat surface. The resulting local supersaturation explains enhanced nucleation phenomena associated with porous silicon. In addition, the selfβaffine fractal surface exhibits quasiβperiodicity that can facilitate longβrange ordering of the nucleated molecules, i.e. the crystallization process. Moreover, small elastic constants of porous silicon are favorable for the surface periodicity tuning to different lattice parameters of growing crystals. The anomalous large scaling range (from silicon interatomic distance up to 100 nm) is favorable for the crystallization of wide range of big macromolecules such as proteins. (Β© 2005 WILEYβVCH Verlag GmbH & Co. KGaA, Weinheim)
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## Abstract Porous silicon (pβSi) has been investigated as a novel delivery system for protein therapeutics. The loading of a model hydrophilic protein, Papain into anodised and stain etched pβSi powders has been investigated using Xβray photoelectron spectroscopy (XPS) and infrared spectroscopy (F