Publication

BPS2025 – Label-free identification of full-length proteins using a nanopore

2025

Abstract

Proteins have critical importance in all cellular processes and are implicated in a plethora of diseases. Methods for proteoform identification are therefore of high interest but are so far struggling e.g., with low efficiency and yield due to complicated analysis protocols. Here, we demonstrate the ability of an aerolysin nanopore to directly identify full length proteins without the need for chemical linkage, or enzymatic sample-processing. By generating a strong electroosmotic flux, we can translocate full length proteins and demonstrate identification at the single-molecule level using machine learning classifiers. In a comparison of signals from seven related proteins of the Turandot family we explore the influence of the analyte's physicochemical properties on the nanopore readout. We anticipate that this in-depth investigation of protein translocations will help to accelerate the path towards fast and simple nanopore based protein identification.

Official source

https://infoscience.epfl.ch/entities/publication/4046c0e5-4db5-44bb-a379-fc64054e83e4

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2025

Abstract

Official source

https://infoscience.epfl.ch/entities/publication/4046c0e5-4db5-44bb-a379-fc64054e83e4

About this result

Related concepts (32)

Fusion protein

Fusion proteins or chimeric (kī-ˈmir-ik) proteins (literally, made of parts from different sources) are proteins created through the joining of two or more genes that originally coded for separate proteins. Translation of this fusion gene results in a single or multiple polypeptides with functional properties derived from each of the original proteins. Recombinant fusion proteins are created artificially by recombinant DNA technology for use in biological research or therapeutics.

Protein

Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity.

Intrinsically disordered proteins

In molecular biology, an intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure, typically in the absence of its macromolecular interaction partners, such as other proteins or RNA. IDPs range from fully unstructured to partially structured and include random coil, molten globule-like aggregates, or flexible linkers in large multi-domain proteins. They are sometimes considered as a separate class of proteins along with globular, fibrous and membrane proteins.