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Related Concept Videos

Dipeptidyl Peptidase 4 Inhibitors01:23

Dipeptidyl Peptidase 4 Inhibitors

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Dipeptidyl peptidase 4 (DPP-4) is a serine protease widely distributed in the body. It's involved in the inactivation of GLP-1 and GIP hormones, which are crucial for insulin regulation. DPP-4 inhibitors, such as sitagliptin (Januvia), saxagliptin (Onglyza), linagliptin (Tradjenta), alogliptin (Nesina), and vildagliptin (Galvus), help increase the proportion of active GLP-1, enhancing insulin secretion. These inhibitors work by competitively binding to DPP-4. This binding causes a...
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Phosphoinositides and PIPs01:42

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Phosphoinositides are a group of phospholipids containing a glycerol backbone with two fatty acid chains and a phosphate attached to a myoinositol sugar ring. The inositol head group extends into the cytoplasm, where it is modified by adding phosphate groups to form phosphatidylinositol phosphates or PIPs.
Different phosphoinositides are synthesized and recruited on the cytosolic face of the plasma membrane. The localization of specific phosphoinositides concentrated in separate membrane...
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A Photocaged N-Phosphonopiperidinone as a Selective Photo-Cleavable DPP8/9 Inhibitor.

Leonard Sewald1, Niko Molke1, Werner W A Tabak1

  • 1Chemical Biology, Center of Medical Biotechnology, Faculty of Biology, University of Duisburg-Essen, Universitätsstr. 2, 45141, Essen, Germany.

Chembiochem : a European Journal of Chemical Biology
|September 12, 2025
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Summary
This summary is machine-generated.

Researchers developed a novel green light-activated photocaged inhibitor for intracellular dipeptidyl peptidases 8 and 9 (DPP8/9). This tool allows precise control over DPP8/9 activity in specific cells, advancing chemical biology and drug discovery.

Keywords:
activity‐based protein profilinginhibitorsphotocageproteasesproteomics

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Area of Science:

  • Chemical Biology
  • Molecular Biology
  • Drug Discovery

Background:

  • Photocaged chemical probes enable spatiotemporal control over biological processes.
  • Intracellular dipeptidyl peptidases 8 and 9 (DPP8/9) are crucial in cell-type-dependent functions, inflammation, and tumorigenesis.
  • Lack of photocaged inhibitors for DPP8/9 hinders their study in complex biological systems.

Purpose of the Study:

  • To develop a novel photocaged inhibitor for DPP8/9.
  • To enable light-triggered, cell-type-specific inhibition of DPP8/9.
  • To validate the inhibitor's utility in biochemical, cellular, and chemical proteomics assays.

Main Methods:

  • Development of a green light-cleavable, BODIPY-photocaged N-phosphono-piperidone-based inhibitor.
  • Assessment of photolysis properties, including phototoxicity.
  • Evaluation of inhibitor potency and selectivity using biochemical, cellular, and chemical proteomics assays, including activity-based protein profiling.

Main Results:

  • Successful development of a green light-cleavable photocaged DPP8/9 inhibitor.
  • Demonstrated low phototoxicity, high potency, and selectivity of the inhibitor.
  • Validation of the inhibitor's suitability for cellular applications and its utility in chemical proteomics.

Conclusions:

  • The developed photocaged inhibitor provides a powerful tool for spatiotemporal control of DPP8/9 activity.
  • This advancement facilitates the investigation of DPP8/9 functions in complex biological models.
  • Chemical proteomics offers a valuable approach for characterizing photocaged compounds.