Binding Constant Determined from the Angstrom-Scale Change in Hydrodynamic Radius of Transferrin upon Binding with Europium Using Dual-Focus Fluorescence Correlation Spectroscopy

2020 ◽  
Vol 11 (3) ◽  
pp. 1148-1153
Author(s):  
Aranyak Sarkar ◽  
Arjun Sharma ◽  
Dibakar Goswami ◽  
Vinu Namboodiri ◽  
Jörg Enderlein ◽  
...  
Keyword(s):  
Fluorescence Correlation Spectroscopy ◽  
Binding Constant ◽  
Hydrodynamic Radius ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation ◽  
Scale Change

scholarly journals Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy

2011 ◽  
Vol 2 ◽  
pp. 374-383 ◽  
Author(s):  
Pauline Maffre ◽  
Karin Nienhaus ◽  
Faheem Amin ◽  
Wolfgang J Parak ◽  
G Ulrich Nienhaus
Keyword(s):  
Fluorescence Correlation Spectroscopy ◽  
Hydrodynamic Radius ◽  
Serum Proteins ◽  
Correlation Spectroscopy ◽  
Fept Nanoparticles ◽  
Absolute Increase ◽  
Fluorescence Correlation ◽  
X Ray Crystallography ◽  
Blood Serum Proteins ◽  
Equilibrium Dissociation

Using dual-focus fluorescence correlation spectroscopy, we have analyzed the adsorption of three human blood serum proteins, namely serum albumin, apolipoprotein A-I and apolipoprotein E4, onto polymer-coated, fluorescently labeled FePt nanoparticles (~12 nm diameter) carrying negatively charged carboxyl groups on their surface. For all three proteins, a step-wise increase in hydrodynamic radius with protein concentration was observed, strongly suggesting the formation of protein monolayers that enclose the nanoparticles. Consistent with this interpretation, the absolute increase in hydrodynamic radius can be correlated with the molecular shapes of the proteins known from X-ray crystallography and solution experiments, indicating that the proteins bind on the nanoparticles in specific orientations. The equilibrium dissociation coefficients, measuring the affinity of the proteins to the nanoparticles, were observed to differ by almost four orders of magnitude. These variations can be understood in terms of the electrostatic properties of the proteins. From structure-based calculations of the surface potentials, positively charged patches of different extents can be revealed, through which the proteins interact electrostatically with the negatively charged nanoparticle surfaces.

Measurement of the Hydrodynamic Radius of Quantum Dots by Fluorescence Correlation Spectroscopy Excluding Blinking

2015 ◽  
Vol 119 (11) ◽  
pp. 4294-4299 ◽  
Author(s):  
A. A. de Thomaz ◽  
D. B. Almeida ◽  
V. B. Pelegati ◽  
H. F. Carvalho ◽  
C. L. Cesar
Keyword(s):  
Quantum Dots ◽  
Fluorescence Correlation Spectroscopy ◽  
Hydrodynamic Radius ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation

scholarly journals Nano-antenna enhanced two-focus fluorescence correlation spectroscopy

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Lutz Langguth ◽  
Agata Szuba ◽  
Sander A. Mann ◽  
Erik C. Garnett ◽  
Gijsje H. Koenderink ◽  
...  
Keyword(s):  
Fluorescence Correlation Spectroscopy ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation
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