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Large and Stable Nanopores Formed by Complement Component 9 for Characterizing Single Folded Proteins.

Wachara Chanakul¹, Anasua Mukhopadhyay^1,2, Saurabh Awasthi¹

¹Adolphe Merkle Institute, University of Fribourg, Fribourg 1700, Switzerland.

|January 28, 2025

Summary

This summary is machine-generated.

Researchers developed a novel biological nanopore using complement component 9 (C9) for precise single-molecule protein analysis. These stable poly(C9) pores accurately determine protein volume, shape, and conformational states.

Keywords:

amphipol change in protein conformation complement component 9 large biological nanopore membrane attack complex protein nanopore resistive pulse recording single-molecule

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Area of Science:

Biophysics
Nanotechnology
Protein analysis

Background:

Biological nanopores are valuable tools for single-molecule analysis.
Existing nanopores face limitations in stability and analyte characterization.

Purpose of the Study:

To introduce and characterize a novel biological nanopore formed by complement component 9 (C9).
To demonstrate the utility of poly(C9) nanopores for accurate single-molecule protein analysis.

Main Methods:

Self-assembly of complement component 9 (C9) to form poly(C9) nanopores.
Resistive pulse recordings to analyze protein volume, shape, and conformation.
Electrolyte solutions with varying ionic strengths and transmembrane voltages were used.

Main Results:

Poly(C9) nanopores are large (10 ± 4 nm diameter, 13 nm length) and stable for 30 minutes.
Analyte proteins were captured via electro-osmotic flow with residence times exceeding 300 μs.
Accurate determination of volume and shape for proteins (9–230 kDa) and distinction between protein conformations (adenylate kinase).

Conclusions:

Poly(C9) nanopores offer a stable and effective platform for single-molecule protein characterization.
This method provides high sensitivity and accuracy for analyzing folded proteins.
The poly(C9) nanopore system advances the capabilities of single-molecule biophysical analysis.