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Activity-based probes for monitoring postproline protease activity

Academic Article
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Overview

related to degree

  • Niessen, Sherry, Ph.D. in Chemistry, Scripps Research 2004 - 2008

authors

  • Sabido, E.
  • Tarrago, T.
  • Niessen, Sherry
  • Cravatt, Benjamin
  • Giralt, E.

publication date

  • September 2009

journal

  • ChemBioChem  Journal

abstract

  • Postproline proteases constitute a subset of serine proteases involved in the regulation of many signaling events and are emerging as promising therapeutic targets for prevalent diseases, such as diabetes and cancer. Therefore, monitoring their activity in different tissues and diverse physiological states would certainly facilitate the elucidation of their physiological role and the establishment of new therapeutic targets. Here, we have synthesized a dipeptidyl phosphonate activity-based probe that has proved to be highly selective for a specific postproline protease, prolyl oligopeptidase (POP). Its high sensitivity allows the detection of the endogenous activity of POP both by in-gel analysis and mass spectrometry. The evidence provided by mass spectrometry for the high selectivity of the synthesized probe opens the possibility of using dipeptidyl phosphonates not only for activity-based profiling (ABP), but also for other ABP applications like substrate-based protease identification.

subject areas

  • Catalytic Domain
  • Mass Spectrometry
  • Organophosphonates
  • Recombinant Proteins
  • Serine Endopeptidases
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Research

keywords

  • activity-based probes
  • peptidomimetics
  • phosphorus
  • prolyl oligopeptidase
  • proteomics
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Identity

PubMed Central ID

  • PMC2847404

International Standard Serial Number (ISSN)

  • 1439-4227

Digital Object Identifier (DOI)

  • 10.1002/cbic.200900244

PubMed ID

  • 19688784
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Additional Document Info

start page

  • 2361

end page

  • 2366

volume

  • 10

issue

  • 14

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