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Real time imaging of protease action on substrates covalently immobilised to polymer supports

Halling, P.J. and Deere, J. and Maltman, B.A. and Flitsch, S.L. and McConnell, G. and Lalaouni, A. (2007) Real time imaging of protease action on substrates covalently immobilised to polymer supports. Advanced Synthesis and Catalysis, 349 (8-9). pp. 1321-1326. ISSN 1615-4150

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Abstract

We report for the first time single bead spatially resolved activity measurements of solid-phase biocatalytic systems followed in real-time. Trypsin cleavage of Bz-Arg-OH and subtilisin cleavage of Z-Gly-Gly-Leu-OH each liberate a free amino group on aminocoumarin covalently immobilised to PEGA1900 beads [a co-polymer of poly(ethylene glycol) with molecular mass of 1900 cross-linked with acrylamide]. This restores fluorescence which is imaged in optical sections by two-photon microscopy. For trypsin cleavage, fluorescence is restricted initially to surface regions, with more than 1 hour needed before reaction is fully underway in the bead centre, presumably reflecting slow enzyme diffusion. In contrast, for subtilisin cleavage fluorescence develops throughout the bead more quickly.

Item type: Article
ID code: 9883
Keywords: protease cleavage, two-photon microscopy , spatial resolution , solid-phase biocatalysis, real-time imaging, Chemistry, Therapeutics. Pharmacology, Organic Chemistry, Catalysis
Subjects: Science > Chemistry
Medicine > Therapeutics. Pharmacology
Department: Faculty of Science > Pure and Applied Chemistry
Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
Unknown Department
Related URLs:
    Depositing user: Strathprints Administrator
    Date Deposited: 28 Nov 2011 15:39
    Last modified: 04 Sep 2014 20:53
    URI: http://strathprints.strath.ac.uk/id/eprint/9883

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