Publications by authors named "Schuyler Corry"
Article Synopsis
- Researchers synthesized special fluorescent β-lactam substrates from cephalosporin to study their interaction with three types of β-lactamase enzymes: TEM-1, p99, and a Bacillus cereus enzyme.
- The most effective substrate used difluorofluorescein linked to two cephalosporin units, ensuring that the final product was a bright fluorescent acid rather than a dimmer compound.
- The hydrolysis rates varied depending on pH and the type of chemical linker used, indicating that the enzyme activity is influenced by these factors; K(m) values for the new substrates were comparable to known values for penicillin G and ampicillin.
To explore the variability in biosensor studies, 150 participants from 20 countries were given the same protein samples and asked to determine kinetic rate constants for the interaction. We chose a protein system that was amenable to analysis using different biosensor platforms as well as by users of different expertise levels. The two proteins (a 50-kDa Fab and a 60-kDa glutathione S-transferase [GST] antigen) form a relatively high-affinity complex, so participants needed to optimize several experimental parameters, including ligand immobilization and regeneration conditions as well as analyte concentrations and injection/dissociation times.
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