Crystallization, X-ray Structure Detemination and Structure-Based Drug Design for Targeted Malarial Enzymes.

Abstract

We have successfully expressed at least six recombinant proteins of the Plasm odium falciparum. We have crystallized and determined the structure of two of these proteins, the lactate dehydrogenase (LDH) and Rab6GTPase. Failure to crystallize other proteins was mostly due to lack of reproducibility in the expression of recombinant proteins. The most important accomplishment came from a collaboration with scientists from WRAIR. We were able to selectively inhibit the P. falciparum LDH in erythrocyte culture without severely affecting the host cells. Our ability to produce sufficient quantities of the active recombinant enzyme and success with obtaining high quality crystals of LDH, encouraged ArQule Inc. to select P. falciparum LDH as a target for developing specific antimalarial agent. According to the agreement between ArQule and us, high throughput screening of ArQule s combinatorial library will be conducted in collaboration with the company. For this purpose, we have adapted an enzyme assay for high throughput screening.

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Document Details

Document Type
Technical Report
Publication Date
Jul 01, 1999
Accession Number
ADA374719

Entities

People

  • Lawrence J. Delucas

Organizations

  • United States Army Medical Research and Development Command

Tags

DTIC Thesaurus Topics

  • Acids
  • Blood
  • Cell Membrane
  • Cells
  • Cellular Structures
  • Chemistry
  • Crystal Structure
  • Crystallization
  • Crystals
  • Cytoplasmic Vesicles
  • Inhibitors
  • Laboratory Animals
  • Malaria
  • Materials
  • Molecules
  • Proteins
  • X Rays

Fields of Study

  • Chemistry

Readers

  • Defense Technology Research and Development.
  • Immunology
  • Parasitology and Pharmacology of Malaria.