Background
Non-invasive planar fluorescence reflectance imaging (FRI) is used for accessing physiological and molecular processes in biological tissue. This method is efficiently used to detect superficial fluorescent inclusions. FRI is based on recording the spatial radiance distribution (SRD) at the surface of a sample. SRD provides information for measuring structural parameters of a fluorescent source (such as radius and depth). The aim of this article is to estimate the depth and radius of the source distribution from SRD, measured at the sample surface. For this reason, a theoretical expression for the SRD at the surface of a turbid sample arising from a spherical light source embedded in the sample, was derived using a steady-state solution of the diffusion equation with an appropriate boundary condition. 相似文献Introduction
The efficacy and the optimal type and volume of aerobic exercise (AE) in fibromyalgia syndrome (FMS) are not established. We therefore assessed the efficacy of different types and volumes of AE in FMS. 相似文献Colloidal nanoparticles (NPs) interact with biological fluids such as human plasma to form a protein coating (corona) on the surface of NPs (NP-protein complex). However, the impact of size and type of NPs on binding of the hard corona to the surface of NPs as well as damping of their optical spectra has not been systematically explored. To elucidate the interaction between biological environment (human plasma) and NPs, a photophysical measurement was conducted to quantify the interaction of two different types of NPs (gold (Au) and silver (Ag)) with common human plasma proteins. The colloidal AuNPs and AgNPs were electrostatically stabilized and varied in diameter from 10 to 80 nm in the presence of common human plasma. The sizes of the NPs were determined using transmission electron microscopy (TEM). Optical absorption spectra were obtained for the complexes. Dynamic light scattering (DLS) measurement and zeta potential were used to characterize the sizes, hydrodynamic diameters, and surface charges of the protein-NPs complexes. Protein separation was performed using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to isolate and identify the protein bands. The absorption of proteins to the NPs was found to be strongly dependent on the size and type of NPs. The distance between surface of NPs by absorbed protein bound to the NPs gradually increased with size of NPs, particularly for AgNPs with primary diameter of < 50 nm. The chi-square test proved that AgNPs are a good candidate in sensing the protein complex in human plasma compared with AuNPs mainly for the AgNPs with diameter sized 50 nm.
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