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Enzymatic Studies of a Malarial Drug Target

MD, PhD, Tina Dasgupta

ISBN 10: 3639130014 / ISBN 13: 9783639130010
Published by VDM Verlag
New Condition: New Soft cover
From BuySomeBooks (Las Vegas, NV, U.S.A.)

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Quantity Available: 20

About this Item

Paperback. 112 pages. Dimensions: 8.7in. x 5.9in. x 0.3in.Plasmodium falciparum is the parasite responsible for more than 90 of deaths caused by the global epidemic of malaria. The enzyme thymidylate synthase- dihydrofolate reductase (TS-DHFR) is a major antimalarial drug target, and mutations in this enzyme have caused widespread resistance. Our work comprises the first systematic, mechanistic characterization of TS-DHFR and its non-active site regions. Our kinetic data show this bifunctional enzyme is regulated by elegant interdomain communication, as well as catalytic contributions from distant structural regions, far from the active sites. Understanding the role of these unique regions may lead to more specific, less toxic therapies. Also, molecular docking and virtual screening of this enzyme identified a lead compound which inhibits both wildtype and drug-resistant parasites. Co-crystal structures of enzyme with compound suggest a molecular basis for overcoming drug resistance. This work demonstrates how in-depth kinetic analyses can be used to identify novel intramolecular targets for rational drug design, and should be useful specially to students of enzymology, protein biochemistry and pharmacology. This item ships from multiple locations. Your book may arrive from Roseburg,OR, La Vergne,TN. Bookseller Inventory # 9783639130010

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Bibliographic Details

Title: Enzymatic Studies of a Malarial Drug Target

Publisher: VDM Verlag

Binding: Paperback

Book Condition:New

Book Type: Paperback

About this title

Synopsis:

Plasmodium falciparum is the parasite responsible for more than 90% of deaths caused by the global epidemic of malaria.The enzyme thymidylate synthase- dihydrofolate reductase (TS-DHFR) is a major antimalarial drug target, and mutations in this enzyme have caused widespread resistance.Our work comprises the first systematic, mechanistic characterization of TS-DHFR and its non-active site regions.Our kinetic data show this bifunctional enzyme is regulated by elegant interdomain communication, as well as catalytic contributions from distant structural regions, far from the active sites. Understanding the role of these unique regions may lead to more specific, less toxic therapies.Also, molecular docking and virtual screening of this enzyme identified a lead compound which inhibits both wildtype and drug-resistant parasites.Co-crystal structures of enzyme with compound suggest a molecular basis for overcoming drug resistance.This work demonstrates how in-depth kinetic analyses can be used to identify novel intramolecular targets for rational drug design, and should be useful specially to students of enzymology, protein biochemistry and pharmacology.

About the Author:

studied Medicine and Pharmacology at Yale University School of Medicine, New Haven, Connecticut, and is currently working as a first-year resident at Memorial Sloan-Kettering Cancer Center in New York, New York.

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