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

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F20%3A00537188" target="_blank" >RIV/68378271:_____/20:00537188 - isvavai.cz</a>

Výsledek na webu

<a href="https://doi.org/10.1002/cbic.202000119" target="_blank" >https://doi.org/10.1002/cbic.202000119</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1002/cbic.202000119" target="_blank" >10.1002/cbic.202000119</a>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10403 - Physical chemistry

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Chembiochem

ISSN

1439-4227

e-ISSN

—

Svazek periodika

21

Číslo periodika v rámci svazku

17

Stát vydavatele periodika

DE - Spolková republika Německo

Počet stran výsledku

7

Strana od-do

2467-2473

Kód UT WoS článku

000531860400001

EID výsledku v databázi Scopus

2-s2.0-85084419085