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Screening Aspartyl Proteases with Combinatorial Libraries

Chapter
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 436)

Abstract

Large numbers of pharmaceutically relevant low-molecular weight compounds can now be synthesized using combinatorial methods. Screening these large libraries of compounds requires high throughput assays. These methods are utilized to search for inhibitors of the aspartyl proteases, plasmepsin II and cathepsin D. Plasmepsin II, a protease found in the malaria parasite, hydrolyzes human hemoglobin, the nutrient source for the parasite and is a new target for anti-malaria therapy. Cathepsin D may be involved in many biological processes and inhibitors would help to clarify the role of cathepsin D in these processes. Plasmepsin II and cathepsin D are ~35% identical in amino acid sequence. Therefore, a comparison of the screening results of these two enzymes will be very useful in determining each enzyme’s specificity and demonstrating the power of utilizing encoded combinatorial libraries.

Keywords

Combinatorial Library Aspartic Proteinase Aspartyl Protease High Throughput Assay Selective Compound 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  1. 1.Pharmacopeia, Inc.PrincetonUSA

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