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Related Experiment Video

Updated: Jan 8, 2026

A Fluorescence-based Assay of Phospholipid Scramblase Activity
09:52

A Fluorescence-based Assay of Phospholipid Scramblase Activity

Published on: September 20, 2016

14.5K

A single vesicle fluorescence microscopy platform to quantify phospholipid scrambling.

Sarina Veit1, Grace I Dearden2, Kartikeya M Menon3

  • 1Department of Molecular Biochemistry, Faculty of Chemistry and Biochemistry, Ruhr University Bochum, Bochum 44801, Germany.

Biorxiv : the Preprint Server for Biology
|December 12, 2025
PubMed
Summary

Researchers developed a new microscopy platform to precisely measure lipid scrambling by individual protein molecules. This reveals significant differences in scramblase activity, crucial for understanding cell membrane transport.

Keywords:
GPCRLarge unilamellar vesicleNBD-phospholipidOpsinProteoliposomeScramblaseTIRF microscopyVDAC

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Related Experiment Videos

Last Updated: Jan 8, 2026

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Biophysics

Background:

  • Scramblases facilitate bidirectional phospholipid transport across cell membranes.
  • Voltage-Dependent Anion Channel 1 (VDAC1) dimers are known to facilitate lipid scrambling.
  • Ensemble measurements obscure individual scramblase activity.

Purpose of the Study:

  • To develop a high-throughput microscopy platform for quantifying single-vesicle lipid scrambling.
  • To investigate the kinetic heterogeneity of VDAC1 dimer scramblase activity.
  • To demonstrate the platform's versatility for studying other scramblases like opsin.

Main Methods:

  • Reconstitution of fluorescently labeled phospholipids and crosslinked VDAC1 dimers into single vesicles.
  • High-throughput single-vesicle imaging to quantify size, protein occupancy, and scrambling rate.
  • Analysis of kinetic heterogeneity in lipid transport mediated by individual VDAC1 dimers.

Main Results:

  • Individual VDAC1 dimers exhibit a wide range of lipid scrambling activities (from <100 to >10,000 lipids/sec).
  • Kinetic heterogeneity in scramblase activity is masked by ensemble measurements.
  • Specific dimer interfaces are identified as critical for rapid lipid scrambling.

Conclusions:

  • The developed microscopy platform enables precise quantification of single-molecule scramblase activity.
  • Significant kinetic heterogeneity exists among VDAC1 dimer scramblases.
  • The platform is versatile for studying transbilayer lipid transport regulation by various scramblases.