title: Photophysics and release kinetics of enzyme-activatable optical probes based on H-dimerized fluorophores on self-immolative linkers.
abstract: A series of activatable optical probes for the model enzyme penicillin G amidase based on intramolecular formation of non-fluorescent H-dimer between two identical dyes were synthesized. The probes are based on a self-immolative linker, which allows positioning both dyes in close spatial proximity to ensure efficient quenching of probes with absorption and fluorescence emission in the near-infrared (NIR) range. A detailed photophysical investigation of the novel optical probes led to a revision of a previously anticipated quenching mechanism and revealed their potential for optimizing the performance of activatable probes based on H-dimer formation. A kinetic analysis indicated that the fluorescence progress curves can be used to qualitatively extract enzyme kinetic parameters.
authors.affiliation: BAM Federal Institute for Materials Research and Testing , D-12489 Berlin, Germany.
authors.forename: Jagoda
authors.initials: J
authors.lastname: Sloniec
authors.forename: Ute
authors.initials: U
authors.lastname: Resch-Genger
authors.forename: Andreas
authors.initials: A
authors.lastname: Hennig
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D019281:Dimerization; D004789:Enzyme Activation; D005456:Fluorescent Dyes / Q000737:chemistry; D007700:Kinetics; D010399:Penicillin Amidase / Q000737:chemistry / Q000378:metabolism*; D010407:Penicillium / Q000201:enzymology; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
chemical_list: D001426:Bacterial Proteins; D005456:Fluorescent Dyes; D010399:Penicillin Amidase