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Peptide and protein loading into porous silicon wafers
Author(s) -
Prestidge C. A.,
Barnes T. J.,
MierczynskaVasilev A.,
Kempson I.,
Peddie F.,
Barnett C.
Publication year - 2008
Publication title -
physica status solidi (a)
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.532
H-Index - 104
eISSN - 1862-6319
pISSN - 1862-6300
DOI - 10.1002/pssa.200723113
Subject(s) - wafer , papain , peptide , secondary ion mass spectrometry , chemistry , silicon , surface roughness , adsorption , materials science , analytical chemistry (journal) , atomic force microscopy , gramicidin , surface finish , chemical engineering , mass spectrometry , chromatography , nanotechnology , composite material , organic chemistry , membrane , biochemistry , engineering , enzyme
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 small hydrophobic peptide) and Papain (a larger hydrophilic protein) were observed (ToF‐SIMS) to penetrate across the entire pSi layer, even at low loading levels. AFM surface imaging of pSi wafers during peptide/protein loading showed that surface roughness increased with Papain loading, but decreased with Gramicidin A loading. For Papain, the loading methodology was also found to influence loading efficiency. These differences indicate more pronounced surface adsorption of Papain. (© 2008 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim)