Single-stranded DNA designed lipophilic G-quadruplexes as transmembrane channels for switchable potassium transport

2019 ◽  
Vol 55 (80) ◽  
pp. 12004-12007 ◽  
Author(s):  
Chunying Li ◽  
Hui Chen ◽  
Li Zhou ◽  
Hui Shi ◽  
Xiaoxiao He ◽  
...  
Keyword(s):  
Ion Channel ◽  
Potassium Transport ◽  
Single Stranded Dna ◽  
G Quadruplex ◽  
Transmembrane Channels

G-quadruplex single-stranded DNA was modified lipophilically and developed as a biomimetic ion channel for selective and switchable K+ transport.

An Ion Transport Switch Based on Light-Responsive Conformation-Dependent G-Quadruplex Transmembrane Channels

2021 ◽  
Author(s):  
Chunying Li ◽  
Hui Chen ◽  
Xiaohai Yang ◽  
Kemin Wang ◽  
Jianbo Liu
Keyword(s):  
Ion Transport ◽  
Selective Transport ◽  
G Quadruplex ◽  
Transmembrane Channels

A light-responsive ion transport switch has been developed based on conformation-dependent azobenzene-incorporated lipophilic G-quadruplex channels, which provides a new smart approach for the selective transport of K+ ions across the...

Discrimination of single‐stranded DNA homopolymers by sieving out G‐quadruplex using tiny solid‐state nanopores

2019 ◽  
Vol 40 (16-17) ◽  
pp. 2117-2124 ◽  
Author(s):  
Wei Si ◽  
Haojie Yang ◽  
Jingjie Sha ◽  
Yin Zhang ◽  
Yunfei Chen
Keyword(s):  
Solid State ◽  
Single Stranded Dna ◽  
G Quadruplex

scholarly journals Human Origin Recognition Complex Binds Preferentially to G-quadruplex-preferable RNA and Single-stranded DNA

2013 ◽  
Vol 288 (42) ◽  
pp. 30161-30171 ◽  
Author(s):  
Shoko Hoshina ◽  
Kei Yura ◽  
Honami Teranishi ◽  
Noriko Kiyasu ◽  
Ayumi Tominaga ◽  
...  
Keyword(s):  
Origin Recognition Complex ◽  
Human Origin ◽  
Single Stranded Dna ◽  
G Quadruplex ◽  
Origin Recognition

Cholinergic Receptor-regulation of Potassium Channels and Potassium Transport in Human Submandibular Acinar Cells

1987 ◽  
Vol 66 (2) ◽  
pp. 541-546 ◽  
Author(s):  
A.P. Morris ◽  
D.V. Gallacher ◽  
C.M. Fuller ◽  
J. Scott
Keyword(s):  
Patch Clamp ◽  
Ion Channel ◽  
Acinar Cells ◽  
Cholinergic Receptor ◽  
Potassium Transport ◽  
Receptor Regulation ◽  
Glandular Tissue ◽  
Stimulus Period ◽  
Stimulus Secretion Coupling

The cholinergic receptor-regulation of K+ transport was studied in human submandibular glands. Acetylcholine stimulation 10 μmol/L results in an increase in membrane permeability (86Rb+ efflux) for, and a net efflux of, K+ ions from the glandular tissue. In the post-stimulus period, there is a net re-uptake of K+ ions into the tissue. Patch-clamp electrophysiological techniques were employed to demonstrate the presence of a large conductance K+ selective ion channel in the basolateral membranes of isolated human submandibular acinar cells. The patch-clamp results indicate that this voltage- and calcium-activated K+ channel operates to regulate the K+ permeability in both the resting and acetylcholine-stimulated acinar cells. We discuss the role of the K+ channel, K+ efflux, and K+ re-uptake in relation to stimulus-secretion coupling.

scholarly journals Common Aspects of G-Quadruplex Destabilization among Helicases and Single Stranded DNA Binding Proteins

2015 ◽  
Vol 108 (2) ◽  
pp. 399a-400a
Author(s):  
Jagat B. Budhathoki ◽  
Sujay Ray ◽  
Pavel Janscak ◽  
Jaya Yodh ◽  
Hamza Balci
Keyword(s):  
Dna Binding ◽  
Binding Proteins ◽  
Dna Binding Proteins ◽  
Single Stranded Dna ◽  
G Quadruplex

scholarly journals POT1 Stability and Binding Measured by Fluorescence Thermal Shift Assays

2021 ◽  
Author(s):  
Lynn W. DeLeeuw ◽  
Robert C. Monsen ◽  
Vytautas Petrauskas ◽  
Robert D. Gray ◽  
Lina Baranauskiene ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Dna Binding ◽  
Competitive Inhibition ◽  
Single Stranded Dna ◽  
Biophysical Characterization ◽  
Drug Candidates ◽  
G Quadruplex ◽  
And Function ◽  
Thermal Shift

AbstractThe protein POT1 (Protection of Telomeres 1) is an integral part of the shelterin complex that protects the ends of human chromosomes from degradation or end fusions. It is the only component of shelterin that binds single-stranded DNA. We describe here the application of two separate fluorescent thermal shift assays (FTSA) that provide quantitative biophysical characterization of POT1 stability and its interactions. The first assay uses Sypro Orange™ and monitors the thermal stability of POT1 and its binding under a variety of conditions. This assay is useful for the quality control of POT1 preparations, for biophysical characterization of its DNA binding and, potentially, as an efficient screening tool for binding of small molecule drug candidates. The second assay uses a FRET-labeled human telomeric G-quadruplex structure that reveals the effects of POT1 binding on thermal stability from the DNA frame of reference. These complementary assays provide efficient biophysical approaches for the quantitative characterization of multiple aspects of POT1 structure and function. The results from these assays provide thermodynamics details of POT1 folding, the sequence selectivity of its DNA binding and the thermodynamic profile for its binding to its preferred DNA binding sequence. Most significantly, results from these assays elucidate two mechanisms for the inhibition of POT1 – DNA interactions. The first is by competitive inhibition at the POT1 DNA binding site. The second is indirect and is by stabilization of G-quadruplex formation within the normal POT1 single-stranded DNA sequence to prevent POT1 binding.

Front Cover: Discrimination of single‐stranded DNA homopolymers by sieving out G‐quadruplex using tiny solid‐state nanopores

2019 ◽  
Vol 40 (16-17) ◽  
Author(s):  
Wei Si ◽  
Haojie Yang ◽  
Jingjie Sha ◽  
Yin Zhang ◽  
Yunfei Chen
Keyword(s):  
Solid State ◽  
Single Stranded Dna ◽  
Front Cover ◽  
G Quadruplex

Interaction of Malachite Green with Guanine-Rich Single-Stranded DNA: Preferential Binding to a G-Quadruplex

2007 ◽  
Vol 119 (48) ◽  
pp. 9465-9467 ◽  
Author(s):  
Achikanath C. Bhasikuttan ◽  
Jyotirmayee Mohanty ◽  
Haridas Pal
Keyword(s):  
Malachite Green ◽  
Single Stranded Dna ◽  
G Quadruplex ◽  
Preferential Binding

Observation of the Coexistence of Sodium and Calcium Ions in a DNA G-Quadruplex Ion Channel

2007 ◽  
Vol 129 (33) ◽  
pp. 10106-10107 ◽  
Author(s):  
Michael P. H. Lee ◽  
Gary N. Parkinson ◽  
Pascale Hazel ◽  
Stephen Neidle
Keyword(s):  
Ion Channel ◽  
Calcium Ions ◽  
G Quadruplex
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