Dynamically Modulating Gating Process of Nanoporous Membrane at Sub-2 Nm Scale

2021 ◽  
Author(s):  
Yahong Zhou ◽  
Junran Hao ◽  
Jiajia Zhou ◽  
Jingwen Liao ◽  
Yan Wei ◽  
...  
Keyword(s):  
Nanoporous Membrane ◽  
Gating Process

Dynamically modulated gating process of nanoporous membrane at sub-2-nm speed

Matter ◽  
2021 ◽  
Author(s):  
Yahong Zhou ◽  
Junran Hao ◽  
Jiajia Zhou ◽  
Jingwen Liao ◽  
Yan Wei ◽  
...  
Keyword(s):  
Nanoporous Membrane ◽  
Gating Process

CAPILLARY EVAPOTRATION ON NANOPOROUS MEMBRANE: A MOLECULAR DYNAMICS STUDY

2019 ◽  
Author(s):  
Ji Li ◽  
Shan Gao ◽  
Wei Liu ◽  
Zhichun Liu
Keyword(s):  
Molecular Dynamics ◽  
Nanoporous Membrane

scholarly journals Modeling Flow in Nanoporous, Membrane Reservoirs and Interpretation of Coupled Fluxes

2014 ◽  
Author(s):  
Filiz Geren ◽  
Tuba Firincioglu ◽  
Caner Karacaer ◽  
Erdal Ozkan ◽  
Chet Ozgen
Keyword(s):  
Nanoporous Membrane ◽  
Modeling Flow

A nanoporous membrane based impedance sensing platform for DNA sensing with gold nanoparticle amplification

2014 ◽  
Vol 193 ◽  
pp. 877-882 ◽  
Author(s):  
Wei Wei Ye ◽  
Jing Yu Shi ◽  
Chun Yu Chan ◽  
Yu Zhang ◽  
Mo Yang
Keyword(s):  
Gold Nanoparticle ◽  
Dna Sensing ◽  
Impedance Sensing ◽  
Nanoporous Membrane ◽  
Sensing Platform

Ion flocculation in water: From bulk to nanoporous membrane desalination

2019 ◽  
Vol 277 ◽  
pp. 516-521 ◽  
Author(s):  
Mateus H. Köhler ◽  
José R. Bordin ◽  
Marcia C. Barbosa
Keyword(s):  
Nanoporous Membrane

Bioinspired Block Copolymer for Mineralized Nanoporous Membrane

ACS Nano ◽  
2018 ◽  
Vol 12 (11) ◽  
pp. 11471-11480 ◽  
Author(s):  
Hui-Jun Zhou ◽  
Guan-Wen Yang ◽  
Yao-Yao Zhang ◽  
Zhi-Kang Xu ◽  
Guang-Peng Wu
Keyword(s):  
Block Copolymer ◽  
Nanoporous Membrane

scholarly journals Electrophoretic Concentration and Electrical Lysis of Bacteria in a Microfluidic Device Using a Nanoporous Membrane

Micromachines ◽  
2017 ◽  
Vol 8 (2) ◽  
pp. 45 ◽  
Author(s):  
Md. Islam ◽  
Ali Shahid ◽  
Kacper Kuryllo ◽  
Yingfu Li ◽  
M. Deen ◽  
...  
Keyword(s):  
Microfluidic Device ◽  
Nanoporous Membrane ◽  
Electrophoretic Concentration ◽  
Electrical Lysis

scholarly journals An Inactivation Stabilizer of the Na+ Channel Acts as an Opportunistic Pore Blocker Modulated by External Na+

2005 ◽  
Vol 125 (5) ◽  
pp. 465-481 ◽  
Author(s):  
Ya-Chin Yang ◽  
Chung-Chin Kuo
Keyword(s):  
Binding Site ◽  
Conformational Changes ◽  
Dissociation Constants ◽  
Channel Gating ◽  
Structural Motif ◽  
Na Channel ◽  
Channel Pore ◽  
Conduction Pathway ◽  
Gating Process ◽  
Pore Blocker

The Na+ channel is the primary target of anticonvulsants carbamazepine, phenytoin, and lamotrigine. These drugs modify Na+ channel gating as they have much higher binding affinity to the inactivated state than to the resting state of the channel. It has been proposed that these drugs bind to the Na+ channel pore with a common diphenyl structural motif. Diclofenac is a widely prescribed anti-inflammatory agent that has a similar diphenyl motif in its structure. In this study, we found that diclofenac modifies Na+ channel gating in a way similar to the foregoing anticonvulsants. The dissociation constants of diclofenac binding to the resting, activated, and inactivated Na+ channels are ∼880 μM, ∼88 μM, and ∼7 μM, respectively. The changing affinity well depicts the gradual shaping of a use-dependent receptor along the gating process. Most interestingly, diclofenac does not show the pore-blocking effect of carbamazepine on the Na+ channel when the external solution contains 150 mM Na+, but is turned into an effective Na+ channel pore blocker if the extracellular solution contains no Na+. In contrast, internal Na+ has only negligible effect on the functional consequences of diclofenac binding. Diclofenac thus acts as an “opportunistic” pore blocker modulated by external but not internal Na+, indicating that the diclofenac binding site is located at the junction of a widened part and an acutely narrowed part of the ion conduction pathway, and faces the extracellular rather than the intracellular solution. The diclofenac binding site thus is most likely located at the external pore mouth, and undergoes delicate conformational changes modulated by external Na+ along the gating process of the Na+ channel.

scholarly journals Label free thrombin detection in presence of high concentration of albumin using an aptamer-functionalized nanoporous membrane

2019 ◽  
Vol 126 ◽  
pp. 88-95 ◽  
Author(s):  
Agnivo Gosai ◽  
Brendan Shin Hau Yeah ◽  
Marit Nilsen-Hamilton ◽  
Pranav Shrotriya
Keyword(s):  
Label Free ◽  
High Concentration ◽  
Nanoporous Membrane
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