Fluorescence Spectroscopy of Lysozyme-Silver Nanoparticles Complex

Identifying the nature of protein-nanoparticle interactions and favored binding sites is an important issue in functional characterization of biomolecules and their physiological responses. Herein, interaction of silver nanoparticles with lysozyme as a model protein has been monitored via fluorescence spectroscopy. Formation of complex between the biomolecule and silver nanoparticles (AgNPs) induced a steady state reduction in the fluorescence intensity of protein at different concentrations of nanoparticles. Tryptophan fluorescence quenching spectra suggested that silver nanoparticles act as a foreign quencher, approaching the protein via this residue. Analysis of the Stern-Volmer plot showed quenching constant of 3.73 μM−1. Moreover, a single binding site in lysozyme is suggested to play role during interaction with AgNPs, having low affinity of binding compared to gold nanoparticles. Unfolding studies of lysozyme showed that complex of lysozyme- AgNPs has not undergone structural perturbations compared to the bare protein. Results of this effort will pave the way for utilization of sensitive spectroscopic techniques for rational design of nanobiomaterials in biomedical applications.

Spectroscopic and SEM Investigation of TCPP in Titanium Matrix

Titanium gels doped with water-soluble cationic porphyrin were synthesized by the sol–gel polymerization of Ti (OC4H9)4. In this work we investigate the spectroscopic properties along with SEM images of tetra carboxyl phenyl porphyrin when incorporated into porous matrix produced by the sol–gel technique.

Automatic Deactivation in Phased Array Probe for Human Prostate Magnetic Resonance Imaging at 1.5T

A four element prototype phased array surface probe has been designed and constructed to improve clinical human prostate spectroscopic data. The probe consists of two pairs of adjacent rectangular coils with an optimum overlap to reduce the mutual inductance. The two pairs are positioned on the anterior and the posterior pelvic region and two couples of varactors at the input of each coil undertake the procedures of tuning and matching. The probe switches off and on automatically during the consecutive phases of the MR experiment with the use of an analog switch that is triggered by a microcontroller. Experimental tests that were carried out resulted in high levels of tuning accuracy. Also, the switching mechanism functions properly for various applied loads and pulse sequence characteristics, producing only 10 μs of latency.

Rigorous Electromagnetic Model of Fourier Transform Infrared (FT-IR) Spectroscopic Imaging Applied to Automated Histology of Prostate Tissue Specimens

Fourier transform infrared (FT-IR) spectroscopic imaging is an emerging technique that provides both chemically and spatially resolved information. The rich chemical content of data may be utilized for computer-aided determinations of structure and pathologic state (cancer diagnosis) in histological tissue sections for prostate cancer. FT-IR spectroscopic imaging of prostate tissue has shown that tissue type (histological) classification can be performed to a high degree of accuracy [1] and cancer diagnosis can be performed with an accuracy of about 80% [2] on a microscopic (≈ 6μm) length scale. In performing these analyses, it has been observed that there is large variability (more than 60%) between spectra from different points on tissue that is expected to consist of the same essential chemical constituents. Spectra at the edges of tissues are characteristically and consistently different from chemically similar tissue in the middle of the same sample. Here, we explain these differences using a rigorous electromagnetic model for light-sample interaction. Spectra from FT-IR spectroscopic imaging of chemically heterogeneous samples are different from bulk spectra of individual chemical constituents of the sample. This is because spectra not only depend on chemistry, but also on the shape of the sample. Using coupled wave analysis, we characterize and quantify the nature of spectral distortions at the edges of tissues. Furthermore, we present a method of performing histological classification of tissue samples. Since the mid-infrared spectrum is typically assumed to be a quantitative measure of chemical composition, classification results can vary widely due to spectral distortions. However, we demonstrate that the selection of localized metrics based on chemical information can make our data robust to the spectral distortions caused by scattering at the tissue boundary.