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Facile synthesis of borofragments and their evaluation in activity-based protein profiling

Academic Article
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Overview

related to degree

  • Cognetta III, Armand B, Ph.D. in Chemical Biology, Scripps Research 2013 - 2018

authors

  • Adachi, S.
  • Cognetta III, Armand B
  • Niphakis, M. J.
  • He, Z.
  • Zajdlik, A.
  • St. Denis, J. D.
  • Scully, C. C. G.
  • Cravatt, Benjamin
  • Yudin, A. K.

publication date

  • 2015

journal

  • Chemical Communications  Journal

abstract

  • The discovery of enzyme inhibitors relies on synthetic methods that enable rapid and modular construction of small molecules. Heterocyclic fragments designed to maximize enthalpic interactions with their protein targets represent a particularly desirable class of molecules. Here we describe a reagent that enables straightforward construction of "borofragments", in which a heterocycle is separated from the boron center by two or three rotatable bonds. The stability of these molecules depends on the MIDA group which likely acts as a slow-release element under biological conditions. Borofragments can be used to discover inhibitors of enzymes that use catalytic oxygen nucleophiles. We have employed this method to identify inhibitors of ABHD10 and the predicted carboxypeptidase CPVL. This technique should be applicable to other classes of targets.

subject areas

  • Boron Compounds
  • Carboxypeptidases
  • Enzyme Inhibitors
  • Esterases
  • Humans
  • Molecular Structure
  • Structure-Activity Relationship
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Identity

PubMed Central ID

  • PMC4330092

International Standard Serial Number (ISSN)

  • 1359-7345

Digital Object Identifier (DOI)

  • 10.1039/c4cc09107h

PubMed ID

  • 25633248
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Additional Document Info

start page

  • 3608

end page

  • 3611

volume

  • 51

issue

  • 17

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