## Abstract The influence of peptide/protein size and hydrophobicity on the physical and chemical aspects of loading within porous silicon (pSi) wafer samples has been determined using Atomic Force Microscopy (AFM) and Time‐of‐Flight Secondary Ion Mass Spectroscopy (ToF‐SIMS). Both Gramicidin A (a
Loading and release of a model protein from porous silicon powders
✍ Scribed by Prestidge, C. A. ;Barnes, T. J. ;Mierczynska-Vasilev, A. ;Skinner, W. ;Peddie, F. ;Barnett, C.
- Book ID
- 105364439
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 142 KB
- Volume
- 204
- Category
- Article
- ISSN
- 0031-8965
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✦ Synopsis
Abstract
Porous silicon (p‐Si) has been investigated as a novel delivery system for protein therapeutics. The loading of a model hydrophilic protein, Papain into anodised and stain etched p‐Si powders has been investigated using X‐ray photoelectron spectroscopy (XPS) and infrared spectroscopy (FTIR) and correlations made with the release kinetics. Variation in specific Papain (Amide I/II) and p‐Si (Si–H~x~ ) functional group absorbances with Papain loading level was characterised using FTIR, while the surface chemical distribution was assessed using XPS. A combination of burst release and sustained release of Papain was observed from p‐Si powders; this was dependent on p‐Si type and the Papain loading level. (© 2007 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)
📜 SIMILAR VOLUMES
## 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 self‐similar surface significa