Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries.

@article{Harris2000RapidAG,
  title={Rapid and general profiling of protease specificity by using combinatorial fluorogenic substrate libraries.},
  author={J. Harris and B. J. Backes and F. Leonetti and S. Mahrus and J. Ellman and C. Craik},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2000},
  volume={97 14},
  pages={
          7754-9
        }
}
  • J. Harris, B. J. Backes, +3 authors C. Craik
  • Published 2000
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences of the United States of America
A method is presented for the preparation and use of fluorogenic peptide substrates that allows for the configuration of general substrate libraries to rapidly identify the primary and extended specificity of proteases. The substrates contain the fluorogenic leaving group 7-amino-4-carbamoylmethylcoumarin (ACC). Substrates incorporating the ACC leaving group show kinetic profiles comparable to those with the traditionally used 7-amino-4-methylcoumarin (AMC) leaving group. The bifunctional… Expand
Protease specificity determination by using cellular libraries of peptide substrates (CLiPS)
Screening combinatorial libraries for optimal enzyme substrates by mass spectrometry.
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