Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Video

Updated: Jun 3, 2026

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Published on: November 1, 2018

Label-free quantification of membrane-ligand interactions using backscattering interferometry.

Michael M Baksh¹, Amanda K Kussrow, Mauro Mileni

¹Department of Chemistry, The Scripps Research Institute, La Jolla, California, USA.

Nature Biotechnology

|March 15, 2011

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Liquid-Phase CO<b><sub>2</sub></b> Capture by a Nonaqueous Cooperative Absorption Mechanism.

Journal of the American Chemical Society·2026

Same author

Characterization Standard for <i>In-situ</i> Cryo-electron Tomography.

bioRxiv : the preprint server for biology·2026

Same author

Orthogonal Chemistry Enables Precision Nanoparticle Cofunctionalization for Tuning Immune Stimulation and Antigen Presentation.

Biomacromolecules·2026

Same author

Biological evaluation of amidine derivatives: In vitro cytotoxicity and cellular antioxidant capacity.

PloS one·2026

Same author

StabLyzeGraph: High-throughput screening of combinatorial mutations using graph neural networks.

Protein science : a publication of the Protein Society·2026

Same author

Tumor agnostic drug delivery with dynamic nanohydrogels.

Nature communications·2026

Same journal

A genome-scale CRISPRi perturbation atlas of human induced pluripotent stem cells.

Nature biotechnology·2026

Same journal

Prime editing for precise genome engineering and modulation of fungal metabolism.

Nature biotechnology·2026

Same journal

Retargeted serine integrases for one-step, precise integration of large DNA sequences in human cells.

Nature biotechnology·2026

Same journal

A retargeted recombinase for precise insertion of large DNA.

Nature biotechnology·2026

Same journal

Experiment-guided AlphaFold3 resolves measurement-consistent protein ensembles.

Nature biotechnology·2026

Same journal

Spatially resolved profiling of extracellular vesicles in tissues with Spatial-EV-seq.

Nature biotechnology·2026

See all related articles

Backscattering interferometry (BSI) offers a new label-free method to measure how strongly drug molecules bind to membrane proteins. This technique accurately quantifies binding affinities in native membranes at picomolar concentrations.

Area of Science:

Biochemistry
Biophysics
Pharmacology

Background:

Membrane proteins are crucial drug targets, but direct, label-free binding measurements are lacking.
Studying ligand interactions with native membrane proteins is essential for drug discovery.

Purpose of the Study:

To introduce and validate backscattering interferometry (BSI) as a method for label-free quantification of ligand-receptor binding to native membranes.
To demonstrate BSI's applicability across diverse membrane environments and molecule types.

Main Methods:

Utilized backscattering interferometry (BSI) to detect minute changes in solution refractive index.
Measured ligand-receptor binding affinities in synthetic and cell-derived membranes.
Quantified binding interactions without the need for labels or supporting substrates.

More Related Videos

Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer

Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer

Published on: October 15, 2015

Related Experiment Videos

Last Updated: Jun 3, 2026

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Dissipative Microgravimetry to Study the Binding Dynamics of the Phospholipid Binding Protein Annexin A2 to Solid-supported Lipid Bilayers Using a Quartz Resonator

Published on: November 1, 2018

Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer

Fluorescence Recovery after Merging a Droplet to Measure the Two-dimensional Diffusion of a Phospholipid Monolayer

Published on: October 15, 2015

Main Results:

BSI accurately quantified ligand-receptor binding affinities in various membrane environments.
Achieved high sensitivity, measuring binding at picomolar concentrations.
Determined equilibrium binding constants across a wide range (micromolar to picomolar) for small and large molecules.

Conclusions:

Backscattering interferometry (BSI) provides a sensitive, label-free method for studying membrane protein-ligand interactions.
BSI's simple, low-cost, and high-sensitivity nature makes it valuable for biochemical and pharmacological research.
This technique facilitates the study of numerous membrane proteins relevant to drug development.