## Abstract The irreversible thrombin inhibitor D‐Phe‐Pro‐Arg‐chloromethylketone (PPACK) was covalently immobilized to PEGylated polymer thin films at its primary α‐amino group. Activity assays and capture of radioconjugated thrombin reveal that the PPACK‐decorated surfaces could bind thrombin form
Serine protease selectivity of the thrombin inhibitor D-Phe-Pro-Agmatine and its homologs
✍ Scribed by Michael R. Wiley; Nickolay Y. Chirgadze; David K. Clawson; Trelia J. Craft; Donetta S. Gifford-Moore; Noel D. Jones; Jennifer L. Olkowski; Aaron L. Schacht; Leonard C. Weir; Gerald F. Smith
- Publisher
- Elsevier Science
- Year
- 1995
- Tongue
- English
- Weight
- 301 KB
- Volume
- 5
- Category
- Article
- ISSN
- 0960-894X
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📜 SIMILAR VOLUMES
An indolizidinone motif with strategically placed substitutents was designed and synthesized as a constrained mimic of D-Phe-Pro-Arg. Low nanomolar inhibition of alpha-thrombin validates the design elements in this inhibitor which also exhibits a 20-fold selectivity for thrombin versus trypsin. An X
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