The preparation of fluorescence-quenched probes for use in the characterization of human factor Xa substrate binding domains.
The preparation and characterization by LCMS of a library of 55 fluorescence- quenched peptides is described. The peptides bear a terminal anthranilamide fluorophore and a penultimate 2,4-dinitrophenyl-L-lysine quencher, and will be used to probe the substrate binding domain of the human blood coagulation enzyme, factor Xa.
Bromfield
Karen M
KM
Centre for Green Chemistry, Monash University, Clayton, Victoria, 3800, Australia.
Cianci
Julia
J
Duggan
Peter J
PJ
D001665:Binding Sites; D015951:Factor Xa / Q000737:chemistry* / Q000378:metabolism; D005453:Fluorescence; D006801:Humans; D008956:Models, Chemical; D015335:Molecular Probes / Q000138:chemical synthesis / Q000737:chemistry; D015394:Molecular Structure; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
D015335:Molecular Probes; D010455:Peptides; D015951:Factor Xa