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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo

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Published on: November 7, 2013

A Robust Immobilization Method for Membrane Protein SPR Assays Using SpyCatcher-SpyTag.

Li Yan^1,2, Chenchen Zhu^2,3, Yingkui Dong^2,4

¹School of Basic Medical Science, Anhui Medical University, Hefei 230032, China.

Analytical Chemistry

|September 1, 2025

Summary

We developed a new method to immobilize membrane proteins in lipid nanodiscs on SPR chips using the SpyCatcher-SpyTag system. This enables stable, real-time analysis of crucial drug target interactions.

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Area of Science:

Biochemistry
Biophysics
Drug Discovery

Background:

Membrane proteins are vital drug targets, but studying their interactions is challenging due to immobilization difficulties.
Surface Plasmon Resonance (SPR) is a key technique, but its use with membrane proteins is hindered by the need for native-like environments.
Lipid nanodiscs provide a native environment, yet stable immobilization on SPR chips remains a hurdle.

Purpose of the Study:

To present a novel, efficient method for covalently immobilizing lipid nanodiscs onto SPR sensor chips.
To enable stable and specific attachment of nanodiscs for reliable membrane protein interaction analysis.
To facilitate kinetic studies of membrane protein-ligand interactions using SPR.

Main Methods:

Utilized the SpyCatcher-SpyTag protein ligation system for covalent immobilization.
Developed a method for attaching lipid nanodiscs containing membrane proteins to SPR sensor surfaces.
Applied the method to study interactions of Granuphilin C2A, GPRC5D, and VDAC1.

Main Results:

Successfully achieved stable and specific covalent immobilization of nanodiscs on SPR chips.
Enabled precise real-time kinetic analysis of membrane protein interactions.
Demonstrated the system's versatility with different membrane proteins and binding partners (lipid, antibody, small molecule).

Conclusions:

The SpyCatcher-SpyTag system offers a convenient and effective approach for nanodisc immobilization on SPR chips.
This method overcomes previous limitations, enhancing SPR's utility for membrane protein studies.
The approach holds significant potential for advancing membrane protein research and accelerating drug discovery.