Controlling protein retention on enzyme-responsive surfaces

Rachel E. Rawsterne, Julie E. Gough, Frank J. M. Rutten, Nhan T. Pham, Wilson C. K. Poon, Sabine L. Flitsch, Beatrice Maltman, Morgan R. Alexander, Rein V. Ulijn

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1505-1511
Number of pages7
JournalSurface and Interface Analysis
Issue number11 special issue
Publication statusPublished - Nov 2006


  • protein retention
  • enzyme-responsive surfaces
  • control
  • responsive surface
  • enzyme
  • biomaterials
  • peptide


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