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- W2036699296 abstract "Significance The exploration of protease substrate specificity is generally restricted to naturally occurring amino acids, limiting the degree of conformational space that can be surveyed. We substantially enhanced this by incorporating 102 unnatural amino acids to explore the S1–S4 pockets of human neutrophil elastase. This approach provides hybrid natural and unnatural amino acid sequences, and thus we termed it the Hybrid Combinatorial Substrate Library. Using this approach, we have designed an extremely active substrate of NE and subsequently converted it into an ultrasensitive activity-based probe for imaging active elastase during the process of neutrophil extracellular trap formation. Our study could have a substantial effect on the design of substrates, inhibitors, and probes for any endopeptidase." @default.
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- W2036699296 date "2014-02-03" @default.
- W2036699296 modified "2023-10-17" @default.
- W2036699296 title "Design of ultrasensitive probes for human neutrophil elastase through hybrid combinatorial substrate library profiling" @default.
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- W2036699296 doi "https://doi.org/10.1073/pnas.1318548111" @default.
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