Label-Free Free-Solution Single-Molecule Protein–Small Molecule Interaction Observed by Double-Nanohole Plasmonic Trapping

ACS Photonics ◽  
2014 ◽  
Vol 1 (5) ◽  
pp. 389-393 ◽  
Author(s):  
Ahmed A. Al Balushi ◽  
Reuven Gordon
Keyword(s):  
Small Molecule ◽  
Single Molecule ◽  
Free Solution ◽  
Label Free ◽  
Molecule Interaction

Label-free free-solution nanoaperture optical tweezers for single molecule protein studies

The Analyst ◽  
2015 ◽  
Vol 140 (14) ◽  
pp. 4760-4778 ◽  
Author(s):  
Ahmed A. Al Balushi ◽  
Abhay Kotnala ◽  
Skyler Wheaton ◽  
Ryan M. Gelfand ◽  
Yashaswini Rajashekara ◽  
...  
Keyword(s):  
Optical Tweezers ◽  
Single Molecule ◽  
Free Solution ◽  
Label Free ◽  
Recent Advances

Recent advances in nanoaperture optical tweezers have enabled studies of single nanoparticles like proteins in label-free, free-solution environments.

Kinetic Capillary Electrophoresis with Mass-Spectrometry Detection (KCE-MS) Facilitates Label-Free Solution-Based Kinetic Analysis of Protein-Small Molecule Binding

ChemBioChem ◽  
2011 ◽  
Vol 12 (17) ◽  
pp. 2551-2554 ◽  
Author(s):  
Jiayin Bao ◽  
Svetlana M. Krylova ◽  
Derek J. Wilson ◽  
Oren Reinstein ◽  
Philip E. Johnson ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Capillary Electrophoresis ◽  
Kinetic Analysis ◽  
Small Molecule ◽  
Free Solution ◽  
Label Free ◽  
Mass Spectrometry Detection ◽  
Kinetic Capillary Electrophoresis

Pre-equilibration kinetic size-exclusion chromatography with mass spectrometry detection (peKSEC-MS) for label-free solution-based kinetic analysis of protein–small molecule interactions

The Analyst ◽  
2015 ◽  
Vol 140 (4) ◽  
pp. 990-994 ◽  
Author(s):  
Jiayin Bao ◽  
Svetlana M. Krylova ◽  
Leonid T. Cherney ◽  
J. C. Yves Le Blanc ◽  
Patrick Pribil ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Kinetic Analysis ◽  
Small Molecule ◽  
Size Exclusion ◽  
Free Solution ◽  
Label Free ◽  
Mass Spectrometry Detection ◽  
Reversible Binding ◽  
Exclusion Chromatography ◽  
Molecule Interactions

Label-free solution-based kinetic analysis of reversible binding between protein and small molecule.

Label-free, mass-sensitive single-molecule imaging using interferometric scattering microscopy

2020 ◽  
Author(s):  
Nikolas Hundt
Keyword(s):  
Single Molecule ◽  
Cellular Systems ◽  
Single Molecule Imaging ◽  
Label Free ◽  
Measurement Sensitivity ◽  
Mass Distributions ◽  
Quantitative Measurements ◽  
Contrast Mechanism ◽  
Cellular Components ◽  
Scattering Signal

Abstract Single-molecule imaging has mostly been restricted to the use of fluorescence labelling as a contrast mechanism due to its superior ability to visualise molecules of interest on top of an overwhelming background of other molecules. Recently, interferometric scattering (iSCAT) microscopy has demonstrated the detection and imaging of single biomolecules based on light scattering without the need for fluorescent labels. Significant improvements in measurement sensitivity combined with a dependence of scattering signal on object size have led to the development of mass photometry, a technique that measures the mass of individual molecules and thereby determines mass distributions of biomolecule samples in solution. The experimental simplicity of mass photometry makes it a powerful tool to analyse biomolecular equilibria quantitatively with low sample consumption within minutes. When used for label-free imaging of reconstituted or cellular systems, the strict size-dependence of the iSCAT signal enables quantitative measurements of processes at size scales reaching from single-molecule observations during complex assembly up to mesoscopic dynamics of cellular components and extracellular protrusions. In this review, I would like to introduce the principles of this emerging imaging technology and discuss examples that show how mass-sensitive iSCAT can be used as a strong complement to other routine techniques in biochemistry.

scholarly journals Critical angle reflection imaging for quantification of molecular interactions on glass surface

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Guangzhong Ma ◽  
Runli Liang ◽  
Zijian Wan ◽  
Shaopeng Wang
Keyword(s):  
Refractive Index ◽  
Small Molecule ◽  
Molecular Interactions ◽  
Glass Surface ◽  
Critical Angle ◽  
Dynamic Range ◽  
Refractive Index Change ◽  
Label Free ◽  
Index Change ◽  
Sensing Range

AbstractQuantification of molecular interactions on a surface is typically achieved via label-free techniques such as surface plasmon resonance (SPR). The sensitivity of SPR originates from the characteristic that the SPR angle is sensitive to the surface refractive index change. Analogously, in another interfacial optical phenomenon, total internal reflection, the critical angle is also refractive index dependent. Therefore, surface refractive index change can also be quantified by measuring the reflectivity near the critical angle. Based on this concept, we develop a method called critical angle reflection (CAR) imaging to quantify molecular interactions on glass surface. CAR imaging can be performed on SPR imaging setups. Through a side-by-side comparison, we show that CAR is capable of most molecular interaction measurements that SPR performs, including proteins, nucleic acids and cell-based detections. In addition, we show that CAR can detect small molecule bindings and intracellular signals beyond SPR sensing range. CAR exhibits several distinct characteristics, including tunable sensitivity and dynamic range, deeper vertical sensing range, fluorescence compatibility, broader wavelength and polarization of light selection, and glass surface chemistry. We anticipate CAR can expand SPR′s capability in small molecule detection, whole cell-based detection, simultaneous fluorescence imaging, and broader conjugation chemistry.

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