Abstract

Nanopores have been proven as versatile single-molecule sensors for individual unlabeled biopolymer detection and characterization. In the present work, a relative large nanopore with a diameter of about 60 nm has been used to detect protein translocation driven by a series of applied voltages. Compared with previous studied small nanopores, a distinct profile of protein translocation through a larger nanopore has been characterized. First, a higher threshold voltage is required to drive proteins into the large nanopore. With the increase of voltages, the capture frequency of protein into the nanopore has been markedly enhanced. And the distribution of current blockage events is characterized as a function of biased voltages. Due to the large dimension of the nanopore, the adsorption and desorption phenomenon of proteins observed with a prolonged dwell time has been weakened in our work. Nevertheless, the protein can still be stretched into an unfolded state by increased electric forces at high voltages. In consideration of the high throughput of the large nanopore, a couple of proteins passing through the nanopore simultaneously occur at high voltage. As a new feature, the feasibility and specificity of a nanopore with distinct geometry have been demonstrated for sensing protein translocation, which broadly expand the application of nanopore devices.

Highlights

  • Over past decades, nanopores have been widely evolved in various devices for investigating unlabeled biopolymers at the single-molecule level [1,2]

  • In summary, electrically facilitated protein translocation through a large nanopore has been investigated in our work

  • A large number of current blockage events are detected above the voltage of 300 mV

Read more

Summary

Introduction

Nanopores have been widely evolved in various devices for investigating unlabeled biopolymers at the single-molecule level [1,2]. The focus is on nucleic acids, proteins are becoming a prime target for investigation [3,4]. Protein transport through the cellular compartments is a very important physiological process for substance and energy metabolism of living cells [5,6,7]. Compared with DNA sequencing, protein translocation through nanopores is more challenging. Proteins have a variety of charge profiles depending on the solvent environment. Each protein has a unique structural architecture, including the primary peptide chain, secondary, tertiary, and quaternary structures, which are responsible for their biological functions.

Methods
Results
Conclusion
Full Text
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