Abstract
A structure- and property-based drug design approach was employed to identify aminooxazoline xanthenes as potent and selective human β-secretase inhibitors. These compounds exhibited good isolated enzyme, cell potency, and selectivity against the structurally related aspartyl protease cathepsin D. Our efforts resulted in the identification of a potent, orally bioavailable CNS penetrant compound that exhibited in vivo efficacy. A single oral dose of compound 11a resulted in a significant reduction of CNS Aβ40 in naive rats.
MeSH terms
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Administration, Oral
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Alzheimer Disease / drug therapy*
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Amyloid Precursor Protein Secretases / antagonists & inhibitors*
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Amyloid beta-Peptides / metabolism
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Animals
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Aspartic Acid Endopeptidases / antagonists & inhibitors*
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Brain / metabolism*
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Cell Line
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Crystallography, X-Ray
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Drug Design
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Humans
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Models, Molecular
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Molecular Structure
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Oxazoles / chemical synthesis*
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Oxazoles / pharmacokinetics
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Oxazoles / pharmacology
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Peptide Fragments / metabolism
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Rats
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Rats, Sprague-Dawley
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Structure-Activity Relationship
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Xanthenes / chemical synthesis*
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Xanthenes / pharmacokinetics
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Xanthenes / pharmacology
Substances
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Amyloid beta-Peptides
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Oxazoles
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Peptide Fragments
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Xanthenes
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amyloid beta-protein (1-40)
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Amyloid Precursor Protein Secretases
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Aspartic Acid Endopeptidases
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BACE1 protein, human
Associated data
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PDB/4FRI
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PDB/4FRJ
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PDB/4FRK