Enzyme screening with synthetic multifunctional pores: Focus on biopolymers
- 6 October 2003
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 100 (21) , 11964-11969
- https://doi.org/10.1073/pnas.2132894100
Abstract
This report demonstrates that a single set of identical synthetic multifunctional pores can detect the activity of many different enzymes. Enzymes catalyzing either synthesis or degradation of DNA (exonuclease III or polymerase I), RNA (RNase A), polysaccharides (heparinase I, hyaluronidase, and galactosyltransferase), and proteins (papain, ficin, elastase, subtilisin, and pronase) are selected to exemplify this key characteristic of synthetic multifunctional pore sensors. Because anionic, cationic, and neutral substrates can gain access to the interior of complementarily functionalized pores, such pores can be the basis for very user-friendly screening of a broad range of enzymes.Keywords
This publication has 39 references indexed in Scilit:
- Synthetic multifunctional pores: lessons from rigid-rod β-barrelsChemical Communications, 2003
- Introduction: ProteasesChemical Reviews, 2002
- Fluorometric Detection of Enzyme Activity with Synthetic Supramolecular PoresScience, 2002
- Hyaluronan Minireview SeriesJournal of Biological Chemistry, 2002
- Synthetic models of cation-conducting channelsChemical Society Reviews, 2001
- Effects of the heparin-mimicking compound RG-13577 on lipoprotein lipase and on lipase mediated binding of LDL to cellsAtherosclerosis, 2001
- Cinderella's Coach Is ReadyScience, 2001
- Ribonuclease AChemical Reviews, 1998
- Mechanistic aspects of DNA polymerases: Escherichia coli DNA polymerase I (Klenow fragment) as a paradigmChemical Reviews, 1990
- Poly-α-amino-acids containing L-Glutamyl Residues as Substrates for PepsinNature, 1962