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Title: DNA G-Wire Formation Using an Artificial Peptide is Controlled by Protease Activity
Authors: Usui, Kenji
Okada, Arisa
Sakashita, Shungo
Shimooka, Masayuki
Tsuruoka, Takaaki
Nakano, Shu-ichi
Miyoshi, Daisuke
Mashima, Tsukasa  kyouindb  KAKEN_id
Katahira, Masato
Hamada, Yoshio
Author's alias: 真嶋, 司
片平, 正人
Keywords: designed peptide
G-wire
G-quadruplex
protease
peptide nucleic acid
PNA
Issue Date: 16-Nov-2017
Publisher: MDPI AG
Journal title: Molecules
Volume: 22
Issue: 11
Thesis number: 1991
Abstract: The development of a switching system for guanine nanowire (G-wire) formation by external signals is important for nanobiotechnological applications. Here, we demonstrate a DNA nanostructural switch (G-wire <--> particles) using a designed peptide and a protease. The peptide consists of a PNA sequence for inducing DNA to form DNA–PNA hybrid G-quadruplex structures, and a protease substrate sequence acting as a switching module that is dependent on the activity of a particular protease. Micro-scale analyses via TEM and AFM showed that G-rich DNA alone forms G-wires in the presence of Ca2+, and that the peptide disrupted this formation, resulting in the formation of particles. The addition of the protease and digestion of the peptide regenerated the G-wires. Macro-scale analyses by DLS, zeta potential, CD, and gel filtration were in agreement with the microscopic observations. These results imply that the secondary structure change (DNA G-quadruplex <--> DNA/PNA hybrid structure) induces a change in the well-formed nanostructure (G-wire <--> particles). Our findings demonstrate a control system for forming DNA G-wire structures dependent on protease activity using designed peptides. Such systems hold promise for regulating the formation of nanowire for various applications, including electronic circuits for use in nanobiotechnologies.
Rights: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
URI: http://hdl.handle.net/2433/233934
DOI(Published Version): 10.3390/molecules22111991
PubMed ID: 29144399
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