Abstract
Recently Eichler and Houghten1 have described the use of a combinatorial peptide library to optimize small trypsin inhibitors. Our kinetic analysis of the most inhibitory peptide, YYGAKIYRPDKM, reveals that it is an inefficiently cleaved substrate for trypsin due to a low kcat. possesses a relatively low KM, and may exhibit nonproductive binding.
Original language | English (US) |
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Pages (from-to) | 611-614 |
Number of pages | 4 |
Journal | Bioorganic and Medicinal Chemistry Letters |
Volume | 5 |
Issue number | 6 |
DOIs | |
State | Published - Mar 16 1995 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Medicine
- Molecular Biology
- Pharmaceutical Science
- Drug Discovery
- Clinical Biochemistry
- Organic Chemistry