Abstract
AbstractThe 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)
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
