Biomedical Spectroscopy and Imaging - Volume 6, issue 3-4
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Biomedical Spectroscopy and Imaging (BSI) is a multidisciplinary journal devoted to the timely publication of basic and applied research that uses spectroscopic and imaging techniques in different areas of life science including biology, biochemistry, biotechnology, bionanotechnology, environmental science, food science, pharmaceutical science, physiology and medicine. Scientists are encouraged to submit their work for publication in the form of original articles, brief communications, rapid communications, reviews and mini-reviews.
The journal is dedicated to providing a single forum for experts in spectroscopy and imaging as applied to biomedical problems, and also for life scientists who use these powerful methods for advancing their research work. BSI aims to promote communication, understanding and synergy across the diverse disciplines that rely on spectroscopy and imaging. It also encourages the submission of articles describing development of new devices and technologies, based on spectroscopy and imaging methods, for application in diverse areas including medicine, biomedical science, biomaterials science, environmental science, pharmaceutical science, proteomics, genomics, metabolomics, microbiology, biotechnology, genetic engineering, nanotechnology, etc.
Abstract: FTIR spectroscopy is an analytical technique widely applied for studying the vibrational fingerprint of organic compounds. In recent years, it has been applied to many biomedical fields because of its potential to detect the composition and molecular structure of various biological materials without the need of probe molecules. The coupling of IR spectrometers with visible microscopes has led to perform the imaging analysis of non-homogeneous samples, such as tissues and cells, in which the biochemical and spatial information are close related. In this review, we report the most significant applications of FTIR to the study of cells in different conditions…(fixed, dried and living) with the aim to monitor their biochemical modifications, either induced or naturally occurring.
Abstract: Background: Due to imperfect slice profiles, unwanted signals from outside the selected voxel may significantly contaminate metabolite signals acquired using in vivo magnetic resonance spectroscopy (MRS). The use of outer volume suppression may exceed the SAR threshold, especially at high field. Objective: We propose using phase-encoding gradients after radiofrequency (RF) excitation to spatially encode unwanted signals originating from outside of the selected single voxel. Methods: Phase-encoding gradients were added to a standard single voxel point-resolved spectroscopy (PRESS) sequence which selects a 2 × 2 × 2 cm3 voxel. Subsequent spatial Fourier transform was used to encode outer volume…signals. Phantom and in vivo experiments were performed using both phase-encoded PRESS and standard PRESS at 7 Tesla. Quantification was performed using fitting software developed in-house. Results: Both phantom and in vivo studies showed that spectra from the phase-encoded PRESS sequence were relatively immune from contamination by oil signals and have more accurate quantification results than spectra from standard PRESS spectra of the same voxel. Conclusion: The proposed phase-encoded single-voxel PRESS method can significantly suppress outer volume signals that may appear in the spectra of standard PRESS without increasing RF power deposition.
Keywords: Single-voxel MRS, phase encoding, outer volume signal, lipid contamination, high field
Abstract: Vacuum-ultraviolet circular dichroism (VUVCD) spectra of malto-, laminari-, isomalto-, and cello-oligosaccharide series and their corresponding polysaccharides (laminarin and dextran) were measured from 200 to 168 nm in aqueous solution at 25°C using a synchrotron-radiation VUVCD spectrophotometer. Disaccharides exhibited markedly different CD spectra depending on the types of glycosidic linkages, and the CD spectra of each oligosaccharide series (with the exception of the isomalto-oligosaccharide series) varied with the chain length below 190 nm while retaining the spectral shape of the constituent disaccharide. These results indicate that the basic structures of oligosaccharides were greatly affected by the configurations of their constituent disaccharides, which had…unique torsion angles restricted by the intramolecular hydrogen bonds between glucose units. Based on comparisons between the experimental and theoretical data, we suggest that the chain-length dependence of CD above 180 nm reflects the backbone structure of oligosaccharides (e.g., helical structures), while those below 180 nm are influenced by other factors associated with higher-energy chromophores such as the hydroxyl groups. The reported comprehensive VUVCD spectra provide basic information for understanding the complicated structures of oligosaccharides in aqueous solution that can be used in their theoretical assignments.
Abstract: Protein small angle scattering (SAS) has become increasing important in structural biochemistry, due to the increased performance and specification of new instruments and advances in the software and hardware used to analyse the data. Whilst all of this is encouraging, there is a lack of standardised experimental methodology within the community. Although a number of protein standards are currently used in SAS experiments to allow accurate molecular weight determination, each has specific advantages and disadvantages. We therefore propose the use of a mutated monomeric enhanced green fluorescent protein, as a protein standard, abbreviated to m-eGFP. It has a number of…advantages over the currently used protein standards, for example it is cheap and easy to produce. It can be expressed in large amounts (> 40 mg/L ) in both hydrogenated and deuterated form. The mutation means it is highly monodisperse and GFP being a beta-barrel structure is thermodynamically stable over a number of days, giving highly reproducible results. We therefore believe m-eGFP is a good protein standard for small angle scattering (SAS).
Keywords: Green fluorescent protein, small angle scattering, protein standard, biophysics, small angle neutron scattering, small angle X-ray scattering
Abstract: Background: We use a temporal template method, the motion history image (MHI), to visualize the hypoperfusion (decreased blood flow) during an acute cerebral ischemic event in a mouse brain. The MHI method was implemented on the dynamic fluorescent (DF) data images. Aims: Our aim was to implement the MHI method on the DF imaging data and visualize the regions where perfusion evolves with time. Methodology: The MHI method was used to process the DF data images recorded during an acute cerebral ischemic event in a mouse brain. Results: We demonstrate that, the MHI images…clearly illustrates the locations where perfusion decreases during occlusion and that is more easily obtained in comparison to a visual inspection of all of the raw DF images constituting the recordings. Conclusion: MHI can be a useful tool for the clinical and research studies.
Keywords: Cerebral blood flow, motion history image, dynamic fluorescent imaging