On selectivity and sensitivity of synthetic multifunctional pores as enzyme sensors: discrimination between ATP and ADP and comparison with biological pores.
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.
Department of Organic Chemistry, University of Geneva, Geneva, Switzerland.
Nathalie
N
Sordé
Stefan
S
Matile
D000244:Adenosine Diphosphate / Q000032:analysis / Q000302:isolation & purification*; D000255:Adenosine Triphosphate / Q000032:analysis / Q000302:isolation & purification*; D000595:Amino Acid Sequence; D001704:Biopolymers / Q000737:chemistry* / Q000378:metabolism; D015374:Biosensing Techniques / Q000379:methods; D004798:Enzymes / Q000032:analysis* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D012680:Sensitivity and Specificity; D013379:Substrate Specificity
D001704:Biopolymers; D004798:Enzymes; D000244:Adenosine Diphosphate; D000255:Adenosine Triphosphate