Total internal reflection fluorescence dynamic

Rotational dynamics of a fluorescent dye adsorbed at the interface provides useful information concerning the rigidity of the microenvironment of liquid-liquid interfaee in terms of the interfacial viscosity. The rotational relaxation time of the rhodamine B dye was studied by time-resolved total internal reflection fluorescent anisotropy. In-plane... 

T. P. Burghardt and D. Axelrod, Total internal reflection/fluorescence photobleaching recovery study of serum albumin adsorption dynamics, Biophys. J. 33, 455-468 (1981). 

Thompson NL, Steele BL. Total internal reflection with fluorescence correlation spectroscopy. Nat. Protoc. 2007 2 878-890. Sund SE, Axelrod D. Actin dynamics at the living cell submembrane imaged by total internal reflection fluorescence photobleach-ing. Biophys. J. 2000 79 1655-1669. 

The use of an evanescent wave to excite fluorophores selectively near a solid-fluid interface is the basis of the technique total internal reflection fluorescence (TIRF). It can be used to study theadsorption kinetics of fluorophores onto a solid surface, and for the determination of orientational order and dynamics in adsorption layers and Langmuir-Blodgett films. TIRF microscopy (TIRFM) may be combined with FRAP ind FCS measurements to yield information about surface diffusion rates and the formation of surface aggregates. 

The three-dimensional network of actin stress fiber, which is an association of actin filaments, provides mechanical support for the cell, determines the cell shape, and enables cell movement. Thus the shape change in the cell due to the laser tsunami can be examined by observing the laser-induced dynamics of fibers. The actin stress fiber was visualized by binding it with enhanced green fluorescence protein (EGFP), and monitored by total internal reflection fluorescence (TIRF) imaging [34]. 

Key words Confocal fluorescence microscopy, Forster resonance energy transfer, Total internal reflection fluorescence microscopy, Single-molecule imaging, GPCR, Heterotrimeric G-proteins, Spatiotemporal dynamics... 

Adsorption dynamics Ruorescence spectroscopy and microscopy (including immunofluorescence, total internal reflection fluorescence) Attenuated total reflection Fourier transform infrared spectroscopy (ATR-FTIR) Quartz crystal microbalance (Spectroscopic) eUipsometry Reflectometric interference spectroscopy... 

In this chapter, electrochemical properties of ET proteins at electrode interfaces studied by spectroelectrochem-ical techniques are described. In situ spectroelectrochemical techniques at well-defined electrode surfaces are sufficiently selective and sensitive to distinguish not only steady state structures and oxidation states of adsorbed species but also dynamics of reactants, products, and intermediates at electrode surfaces on a monolayer level. The spectroelectrochemical techniques used in studies of ET proteins include IR reflection-absorption, potential-modulated UV-vis reflectance (electroreflectance), surface-enhanced Raman scattering (SERS) and surface plasmon resonance, total internal reflection fluorescence, (TIRE) and absorbance linear dichroism spectroscopies. 

Rotational dynamics of a fluorescent dye adsorbed at the interface provides useful information concerning the rigidity of the microenvironment of liquid-liquid interface in terms of the interfacial viscosity. The rotational relaxation time of the rhodamine B dye was studied by the time-resolved total internal reflection fluorescent anisotropy. In-plane rotational relaxation time of octadecylrhodamine B cation was evaluated under the presence or absence of a surfactant [26]. Table 2.8 shows that by adding a surfactant, the relaxation time and the interfadal viscosity increased. Anionic surfactants SDS and HDHP (hydrogen dihexadecylphosphate) were more effective in reducing the rotational motion, because of the electrostatic interaction. HDHP with double long chains hindered the interfacial rotation more [40]. 

Thompson NL, Burghardt TP, Axelrod D (1981) Measuring surface dynamics of biomolecules by total internal reflection fluorescence with photobleaching recovery or correlation spectroscopy. Biophys J 33(3) 435 54... 

Thompson, N. L. Burghardt, T. P. Axelrod, D. Measuring Surface Dynamics of Biomolecules by Total Internal-Reflection Fluorescence with Photobleaching Recovery or Correlation Spectroscopy. Biophys. J. 1981, 33, 435 54. 

M. Yanagimachi, N. Tamai, and H. Masuhara, Chem. Phys. Lett., 200, 469 (1992). Solvation Dynamics of a Coumarin Dye at Liquid Solid Interface Layer - Picosecond Total Internal-Reflection Fluorescence Spectroscopic Study. 

T. Yamashita, T. Uchida, T. Fukushima, andN. Teramae,/. Phys. Chem. B, 107,4786 (2003). Solvation Dynamics of Fluorophores with an Anthroyloxy Group at the Heptane/Water Interface as Studied by Time-Resolved Total Internal Reflection Fluorescence Spectroscopy. 

A. Itaya, A. Kurahashi, H. Masuhara, N. Tamai, and I. Yamazaki, Dynamic fluorescence microprobe method utilizing total internal reflection phenomena, Chem. Lett. 1987, 1079-1082. 

It is well known that both nanometre and nanosecond-picosecond resolutions at an interface can be achieved by total internal reflection (TIR) fluorescence spectroscopy. Unlike steady-state fluorescence spectroscopy, fluorescence dynamics is highly sensitive to microscopic environments, so that time-resolved TIR fluorometry at water/oil interfaces is worth exploring to obtain a clearer picture of the interfacial phenomena [1]. One of the interesting targets to be studied is the characteristics of dynamic motions of a molecule adsorbed on a water/oil interface. Dynamic molecular motions at a liquid/liquid interface are considered to be influenced by subtle changes in the chemical/physical properties of the interface, particularly in a nanosecond-picosecond time regime. Therefore, time-resolved spectroscopy is expected to be useful to study the nature of a water/oil interface. 

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