scholarly journals Front Cover: Validation of the Slow Off‐Kinetics of Sirtuin‐Rearranging Ligands (SirReals) by Means of Label‐Free Electrically Switchable Nanolever Technology (ChemBioChem 8/2020)

ChemBioChem ◽  
2020 ◽  
Vol 21 (8) ◽  
pp. 1050-1050
Author(s):  
Matthias Schiedel ◽  
Herwin Daub ◽  
Aymelt Itzen ◽  
Manfred Jung
Keyword(s):  
Label Free ◽  
Front Cover ◽  
Kinetics Of

scholarly journals Validation of the Slow Off‐Kinetics of Sirtuin‐Rearranging Ligands (SirReals) by Means of Label‐Free Electrically Switchable Nanolever Technology

ChemBioChem ◽  
2020 ◽  
Vol 21 (8) ◽  
pp. 1161-1166 ◽  
Author(s):  
Matthias Schiedel ◽  
Herwin Daub ◽  
Aymelt Itzen ◽  
Manfred Jung
Keyword(s):  
Label Free ◽  
Kinetics Of

scholarly journals Front Cover: Charge‐Transfer Kinetics of The Solid‐Electrolyte Interphase on Li 4 Ti 5 O 12 Thin‐Film Electrodes (ChemSusChem 16/2020)

ChemSusChem ◽  
2020 ◽  
Vol 13 (16) ◽  
pp. 3941-3941
Author(s):  
Ralph Nicolai Nasara ◽  
Wen Ma ◽  
Yasuyuki Kondo ◽  
Kohei Miyazaki ◽  
Yuto Miyahara ◽  
...  
Keyword(s):  
Thin Film ◽  
Charge Transfer ◽  
Solid Electrolyte ◽  
Solid Electrolyte Interphase ◽  
Front Cover ◽  
Thin Film Electrodes ◽  
Kinetics Of

scholarly journals High-Resolution Adhesion Kinetics of EGCG-Exposed Tumor Cells on Biomimetic Interfaces: Comparative Monitoring of Cell Viability Using Label-Free Biosensor and Classic End-Point Assays

ACS Omega ◽  
2018 ◽  
Vol 3 (4) ◽  
pp. 3882-3891 ◽  
Author(s):  
Beatrix Peter ◽  
Rita Ungai-Salanki ◽  
Bálint Szabó ◽  
Agoston G. Nagy ◽  
Inna Szekacs ◽  
...  
Keyword(s):  
High Resolution ◽  
Cell Viability ◽  
Tumor Cells ◽  
Label Free ◽  
End Point ◽  
Biomimetic Interfaces ◽  
Kinetics Of

scholarly journals Single-cell adhesion force kinetics of cell populations from combined label-free optical biosensor and robotic fluidic force microscopy

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Milan Sztilkovics ◽  
Tamas Gerecsei ◽  
Beatrix Peter ◽  
Andras Saftics ◽  
Sandor Kurunczi ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Single Cell ◽  
Temporal Resolution ◽  
Adhesion Force ◽  
Optical Biosensor ◽  
Cell Populations ◽  
Label Free ◽  
Kinetic Evaluation ◽  
Force Microscopy ◽  
Kinetics Of

AbstractSingle-cell adhesion force plays a crucial role in biological sciences, however its in-depth investigation is hindered by the extremely low throughput and the lack of temporal resolution of present techniques. While atomic force microcopy (AFM) based methods are capable of directly measuring the detachment force values between individual cells and a substrate, their throughput is limited to few cells per day, and cannot provide the kinetic evaluation of the adhesion force over the timescale of several hours. In this study a high spatial and temporal resolution resonant waveguide grating based label-free optical biosensor was combined with robotic fluidic force microscopy to monitor the adhesion of living cancer cells. In contrast to traditional fluidic force microscopy methods with a manipulation range in the order of 300–400 micrometers, the robotic device employed here can address single cells over mm-cm scale areas. This feature significantly increased measurement throughput, and opened the way to combine the technology with the employed microplate-based, large area biosensor. After calibrating the biosensor signals with the direct force measuring technology on 30 individual cells, the kinetic evaluation of the adhesion force and energy of large cell populations was performed for the first time. We concluded that the distribution of the single-cell adhesion force and energy can be fitted by log-normal functions as cells are spreading on the surface and revealed the dynamic changes in these distributions. The present methodology opens the way for the quantitative assessment of the kinetics of single-cell adhesion force and energy with an unprecedented throughput and time resolution, in a completely non-invasive manner.

Label-free detection of early oligomerization of α-synuclein and its mutants A30P/E46K through solid-state nanopores

Nanoscale ◽  
2019 ◽  
Vol 11 (13) ◽  
pp. 6480-6488 ◽  
Author(s):  
Xiaoqing Li ◽  
Xin Tong ◽  
Wenlong Lu ◽  
Dapeng Yu ◽  
Jiajie Diao ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Solid State ◽  
Time Dependent ◽  
Label Free ◽  
Label Free Detection ◽  
Kinetics Of

Time-dependent kinetics of early oligomerization of Parkinson's disease-related α-synuclein and its mutants A30P/E46K have been studied through solid-state nanopores.

scholarly journals Grating-coupled interferometry reveals binding kinetics and affinities of Ni ions to genetically engineered protein layers

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Hajnalka Jankovics ◽  
Boglarka Kovacs ◽  
Andras Saftics ◽  
Tamas Gerecsei ◽  
Éva Tóth ◽  
...  
Keyword(s):  
Binding Sites ◽  
Kinetic Data ◽  
Specific Binding ◽  
Genetically Engineered ◽  
Binding Kinetics ◽  
Titration Calorimetry ◽  
Affinity Binding ◽  
Label Free ◽  
Low Protein ◽  
Kinetics Of

AbstractReliable measurement of the binding kinetics of low molecular weight analytes to their targets is still a challenging task. Often, the introduction of labels is simply impossible in such measurements, and the application of label-free methods is the only reliable choice. By measuring the binding kinetics of Ni(II) ions to genetically modified flagellin layers, we demonstrate that: (1) Grating-Coupled Interferometry (GCI) is well suited to resolve the binding of ions, even at very low protein immobilization levels; (2) it supplies high quality kinetic data from which the number and strength of available binding sites can be determined, and (3) the rate constants of the binding events can also be obtained with high accuracy. Experiments were performed using a flagellin variant incorporating the C-terminal domain of the nickel-responsive transcription factor NikR. GCI results were compared to affinity data from titration calorimetry. We found that besides the low-affinity binding sites characterized by a micromolar dissociation constant (Kd), tetrameric FliC-NikRC molecules possess high-affinity binding sites with Kd values in the nanomolar range. GCI enabled us to obtain real-time kinetic data for the specific binding of an analyte with molar mass as low as 59 Da, even at signals lower than 1 pg/mm2.

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