BACE inhibitors and their use in the treatment of Alzheimer'sDisease
BACE (beta-site of APP cleaving enzyme) is a criticalcomponent in Alzheimer's Disease (AD), and the development of BACEinhibitors shows great potential as a therapy for the disease.BACE: Lead Target for Orchestrated Therapy of Alzheimer'sDisease covers virtually all aspects of BACE from initialidentification, discovery of inhibitors, and challenges in clinicaldevelopment, while providing a global understanding essential forproductive and successful drug discovery.
This book details the story of the discovery of BACE and itsrole in AD and comprehensively discusses:
* The development of BACE inhibitors as therapeutics forAlzheimer's disease
* The research that led to the identification of BACE
* New BACE inhibitors currently being clinically tested
* ADME (absorption, distribution, metabolism, excretion) andclinical trial design--topics not addressed in current fieldliterature
* Cutting-edge technology such as high-throughput screening,structure-based drug design, and QSAR in context of BACE inhibitorsand Alzheimer's drug discovery
* Other approaches to BACE inhibition based on interaction withthe precursor protein APP
By enhancing the reader's understanding of the various aspectsof the BACE drug-discovery process, this much-needed reference willserve as a key resource for all scientists involved in Alzheimer'sresearch--and inspire new approaches to treatment of AD.
Varghese John
Alzheimersche Krankheit Biowissenschaften Chemie Chemistry Drug Discovery & Development Life Sciences Medical Science Medizin Neuroscience Neurowissenschaften Pharmacology & Pharmaceutical Medicine Pharmakologie u. Pharmazeutische Medizin Wirkstoffforschung Wirkstoffforschung u. -entwicklung
"Overall this book is a timely and comprehensive resource coveringdevelopments in BACE-targeted therapeutic agents from infancy tothe present time. It will prove to be valuable to researchersworking in the AD field, as well as to medicinal chemists seekingto learn more about rational design of aspartyl proteaseinhibitors." (ChemMedChem, November 2010)
()