Abstract
An NMR fragment screen for binders to the bromodomains of BRD4 identified 2-methyl-3-ketopyrroles 1 and 2. Elaboration of these fragments guided by structure-based design provided lead molecules with significant activity in a mouse tumor model. Further modifications to the methylpyrrole core provided compounds with improved properties and enhanced activity in a mouse model of multiple myeloma.
Keywords:
BET proteins; Bromodomain; Fragment screening.
Copyright © 2017 Elsevier Ltd. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Animals
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Antineoplastic Agents / chemical synthesis
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Antineoplastic Agents / chemistry*
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Antineoplastic Agents / pharmacokinetics
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Antineoplastic Agents / therapeutic use
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Binding Sites
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Cell Line, Tumor
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Cell Proliferation / drug effects
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Crystallography, X-Ray
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Drug Design
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Half-Life
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Humans
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Mice
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Molecular Dynamics Simulation
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Multiple Myeloma / drug therapy
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Nuclear Proteins / antagonists & inhibitors*
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Nuclear Proteins / metabolism
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Pyrroles / chemical synthesis
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Pyrroles / chemistry*
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Pyrroles / pharmacokinetics
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Pyrroles / therapeutic use
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Structure-Activity Relationship
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Transcription Factors / antagonists & inhibitors*
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Transcription Factors / metabolism
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Transplantation, Heterologous
Substances
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Antineoplastic Agents
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Brd4 protein, mouse
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Nuclear Proteins
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Pyrroles
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Transcription Factors