Single-molecule study of peptides with the same amino acid composition but different sequences by using an aerolysin nanopore

0537188 - FZÚ 2021 RIV DE eng J - Journal Article
Hu, F. - Angelov, Borislav - Li, S. - Li, N. - Lin, X. - Zou, A.
Single-molecule study of peptides with the same amino acid composition but different sequences by using an aerolysin nanopore.
Chembiochem. Roč. 21, č. 17 (2020), s. 2467-2473. ISSN 1439-4227. E-ISSN 1439-7633
Institutional support: RVO:68378271
Keywords : aerolysin nanopore * single-molecule detection * model peptides * folding * hydrogen bond
OECD category: Physical chemistry
Impact factor: 3.164, year: 2020
Method of publishing: Limited access
https://doi.org/10.1002/cbic.202000119

Nanopores are original sensors employed for highly sensitive peptides/proteins detection. Herein, we describe the use of an aerolysin nanopore to identify two similar model peptides, YEQYEQQDDDRQQQ (YEQ2Q3) and QDDDRQQQYEQYEQ (Q3YEQ2), with the same amino acid composition but different sequences. All-atom molecular dynamics (MD) simulations reveal that YEQ2Q3 possesses fewer hydrogen bonds and a more extended conformation than Q3YEQ2. These two peptides, which fold differently, exhibit obviously distinct mass-independent current blockades with characteristic dwell times when entering the aerolysin nanopore. Typically, at +60 mV, the statistical dwell time of 0.630 +/- 0.018 ms for peptide Q3YEQ2 is four times longer than the value of 0.160 +/- 0.001 ms for peptide YEQ2Q3, and yet peptide YEQ2Q3 induces similar to 1.9 % larger blockade current amplitude than peptide Q3YEQ2.
Permanent Link: http://hdl.handle.net/11104/0314931