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Related Concept Videos

Protein Dynamics in Living Cells01:19

Protein Dynamics in Living Cells

Different fluorescence-based techniques are used to study the protein dynamics in living cells. These techniques include FRAP, FRET, and PET.
Fluorescent recovery after photobleaching (FRAP) is a fluorescent-protein-based detection technique used to quantify protein movement rates within the cell. This method exposes a small portion of the cell to an intense laser beam. The laser beam causes permanent photobleaching of the fluorophore-tagged proteins in the exposed region. As the bleached...

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Related Experiment Video

Updated: Jun 23, 2026

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells
11:06

Multi-color Localization Microscopy of Single Membrane Proteins in Organelles of Live Mammalian Cells

Published on: June 30, 2018

Multifunctional prenylated peptides for live cell analysis.

James W Wollack1, Nicholette A Zeliadt, Daniel G Mullen

  • 1Department of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455, USA.

Journal of the American Chemical Society
|May 12, 2009
PubMed
Summary
This summary is machine-generated.

Researchers developed fluorescent peptides to track protein prenylation in living cells. These peptides enter cells and localize near the nucleus, aiding studies of prenylation and intracellular trafficking.

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Last Updated: Jun 23, 2026

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Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Background:

  • Protein prenylation is a crucial post-translational modification in eukaryotic cells, regulating signal transduction pathways.
  • Inhibition of protein prenylation shows therapeutic potential, but in vitro studies limit understanding of its in vivo localization.
  • Studying prenylation in living cells is essential for comprehending its biological roles and developing targeted therapies.

Purpose of the Study:

  • To synthesize and analyze fluorescently labeled peptides for studying protein prenylation in living cells.
  • To investigate the intracellular localization and trafficking of prenylated peptides.
  • To establish a synthetic strategy for creating peptides with acid-sensitive functionalities.

Main Methods:

  • Development of a synthetic route for multifunctional peptides incorporating fluorophores and cell-penetrating sequences (e.g., penetratin).
  • Utilized a novel Acm to Scm protecting group conversion compatible with acid-sensitive isoprenoid moieties.
  • Live cell imaging to analyze peptide uptake mechanisms and intracellular localization based on prenylation and penetratin presence.

Main Results:

  • Synthesized fluorescent peptides based on the CDC42 protein C-terminus, enabling live cell analysis of prenylation.
  • Demonstrated that prenylated peptides, even with a full CAAX box, can enter cells independently of penetratin.
  • Observed energy-independent cell entry and perinuclear localization of prenylated peptides lacking penetratin.

Conclusions:

  • Developed peptides provide a novel tool for investigating protein prenylation dynamics and localization within living cells.
  • The synthetic methodology is versatile for assembling peptides with acid-sensitive groups, expanding possibilities for chemical biology research.
  • These findings facilitate future studies on enzymatic processing and intracellular trafficking of prenylated molecules.