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On selectivity and sensitivity of synthetic multifunctional pores as enzyme sensors: Discrimination between ATP and ADP and comparison with biological pores
Author(s) -
Sordé Nathalie,
Matile Stefan
Publication year - 2004
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.10573
Subject(s) - chemistry , melittin , selectivity , glucose 6 phosphate isomerase , phosphofructokinase , hexokinase , enzyme , combinatorial chemistry , papain , glycolysis , biochemistry , catalysis , peptide
This report delineates scope and limitation of the selectivity of synthetic multifunctional pores as enzyme sensors using glycolytic enzymes as example (G. Das, P. Talukdar, and S. Matile, Science, 2002, Vol. 298, pp. 1600–1602). Unproblematic detectability of hexokinase and phosphofructokinase demonstrates that the selectivity of synthetic multifunctional pore (SMPs) sensors suffices to sense ATP in mixed analytes containing ADP, whereas detection of the isomerization of glucose 6‐phosphate into fructose 6‐phosphate by phosphoglucose isomerase is not possible with confidence. The sensitivity of SMP sensors is sufficient for end‐point detection of one picomole poly‐ L ‐glutamate hydrolyzed by papain in unoptimized assay format; the sensitivity of melittin as representative biological pore of similar charge and aggregation number to detect the same reaction is more than four orders of magnitude inferior. © 2004 Wiley Periodicals, Inc. Biopolymers (Pept Sci) , 2004