Journal
SURFACE AND INTERFACE ANALYSIS
Volume 38, Issue 11, Pages 1505-1511Publisher
JOHN WILEY & SONS LTD
DOI: 10.1002/sia.2492
Keywords
biomaterials; peptide; responsive surface; enzyme
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Funding
- Engineering and Physical Sciences Research Council [GR/S10377/01] Funding Source: researchfish
- Wellcome Trust [072864] Funding Source: Medline
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The ability to change the properties of solid surfaces on demand is a key component of a multitude of established and emerging technologies. Stimuli that have previously been used to trigger changes in surface properties include changes in solvent, light, pH, ionic strength, temperature and magnetic or electric fields. We are interested in developing surfaces that can be triggered by the catalytic action of enzymes. We demonstrate the selective protease (alpha-chymotrypsin and thermolysin) catalysed peptide hydrolysis of surface-tethered fluorenylmethoxycarbonyl-dipeptides. We highlight some of the challenges evident from surface analysis in overcoming enzyme retention to the surface addressed by physical adsorption of soluble PEG(200) to the surface prior to enzyme exposure. Analysis by ToF-SIMS and XPS shows that a-chymotrypsin is deposited and retained on the surfaces and that thermolysin, a much more stable enzyme, selectively cleaves the tethered peptides as intended, and is removed from the surface by washing. Copyright (C) 2006 John Wiley & Sons, Ltd.
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