Protein Unfolding Through Nanopores

Title:Protein Unfolding Through Nanopores

Volume: 21 Issue: 3

Author(s): Abdelghani Oukhaled, Manuela Pastoriza-Gallego, Laurent Bacri, Jerome Mathe, Loic Auvray and Juan Pelta

Affiliation:

Keywords: Aerolysin, α-hemolysin, first order transition, nanopore, protein denaturation, protein folding, single molecule experiment.

Abstract: In this mini-review we introduce and discuss a new method, at single molecule level, to study the protein folding and protein stability, with a nanopore coupled to an electric detection. Proteins unfolded or partially folded passing through one channel submitted to an electric field, in the presence of salt solution, induce different detectable blockades of ionic current. Their duration depends on protein conformation. For different studies proteins through nanopores, completely unfolded proteins induce only short current blockades. Their frequency increases as the concentration of denaturing agent or temperature increases, following a sigmoidal denaturation curve. The geometry or the net charge of the nanopores does not alter the unfolding transition, sigmoidal unfolding curve and half denaturing concentration or half temperature denaturation. A destabilized protein induces a shift of the unfolding curve towards the lower values of the denaturant agent compared to the wild type protein.Partially folded proteins exhibit very long blockades in nanopores. The blockade duration decreases when the concentration of denaturing agent increases. The variation of these blockades could be associated to a possible glassy behaviour.

Cite this article as:

Oukhaled Abdelghani, Pastoriza-Gallego Manuela, Bacri Laurent, Mathe Jerome, Auvray Loic and Pelta Juan, Protein Unfolding Through Nanopores, Protein & Peptide Letters 2014; 21 (3) . https://dx.doi.org/10.2174/09298665113209990080