Abstract
Enzyme protection: An irreversible solid-phase, aqueous peptide coupling resulted in the formation of a library of eight dipeptides, while an irreversible protease-catalyzed hydrolysis destroyed them. Those dipeptides that bound to carbonic anhydrase were protected from destructions. Six cycles of active ester addition produced only the best-binding dipeptide (> 100:1) in 29% yield.
Original language | English (US) |
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Pages (from-to) | 2432-2436 |
Number of pages | 5 |
Journal | Angewandte Chemie - International Edition |
Volume | 43 |
Issue number | 18 |
DOIs | |
State | Published - Apr 26 2004 |
Keywords
- Combinatorial chemistry
- Drug design
- Enzyme inhibitors
- Kinetics
- Receptors