In:
Surface and Interface Analysis, Wiley, Vol. 38, No. 11 ( 2006-11), p. 1505-1511
Abstract:
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 (α‐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 α‐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 © 2006 John Wiley & Sons, Ltd.
Type of Medium:
Online Resource
ISSN:
0142-2421
,
1096-9918
Language:
English
Publisher:
Wiley
Publication Date:
2006
detail.hit.zdb_id:
2023881-2
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