Abstract
The structures of protein are diverse and closely related to their physiological functions. Elucidating the mechanisms of protein folding and function remains a prominent challenge in biophysics. Intrinsically disordered proteins (IDPs) are a class of proteins lacking an ordered structure and related to a wide range of diseases such as Alzheimer's disease, Parkinson's disease, cancer, and diabetes, leading to the urgent need to develop powerful methods to characterize the interaction between the structure change and physiological function of these proteins. As a sensitive single-molecule approach, the super-confined aerolysin nanopore has been applied in peptide detection. In order to understand the mechanisms of IDPs folding and function, here, a controlled single-molecule interface of aerolysin nanopore was employed to investigate the protein structural ensembles upon interaction with the environment. We selected the Aβ25-35 fragment with similar physiological functions as β-amyloid peptide 42 (Aβ42) that associates with Alzheimer’s disease as an example to clarify its structural changes in aqueous solution in real-time through the aerolysin nanopore. The dynamic conformation change of peptide in solution can be monitored in real-time via the current blockades and duration time. It can be observed that the conformation of Aβ25-35 changed from random coil to β-sheet. This study facilitates the label-free detection of the dynamic structural changes of IDPs at the single-molecule level rather than measuring the average properties of a protein sample, which has the potential to further make a significant contribution to solving the questions concerning the structure and function of IDPs.
Published Version (
Free)
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a call