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Important Biomolecules (important + biomolecule)
Selected AbstractsEffect of mangiferin on radiation-induced micronucleus formation in cultured human peripheral blood lymphocytesENVIRONMENTAL AND MOLECULAR MUTAGENESIS, Issue 1 2005Ganesh Chandra Jagetia Abstract Irradiation causes a variety of lesions in important biomolecules of the cell through generation of free radicals leading to genomic instability. DNA strand breaks, acentric fragments, or defective kinetochores are manifested as micronuclei after the first cell division. Chemicals that can trap free radicals may reduce the deleterious effects of ionizing radiation. Mangiferin (MGN), a glucosylxanthone derived from Mangifera indica (mango), was investigated for its ability to reduce the frequency of radiation-induced micronucleated binucleate cells (MNBNCs) in cultured human peripheral blood lymphocytes (HPBLs). HPBL cultures were pretreated with 0, 5, 10, 20, 50, and 100 ,g/ml of MGN for 30 min before exposure to 3 Gy of 60Co ,-radiation. The maximum decline in radiation-induced micronuclei was observed at a concentration of 50 ,g/ml MGN; thereafter, a nonsignificant elevation in MNBNC frequency was observed at 100 ,g/ml MGN. Since the lowest MNBNC frequency was observed for 50 ,g/ml MGN, dose-response studies were undertaken using this concentration. Irradiation of HPBLs with 0, 1, 2, 3, or 4 Gy of ,-radiation caused a dose-dependent elevation in the MNBNC frequency, while treatment of HPBLs with 50 ,g/ml MGN 30 min before radiation resulted in significant declines in these frequencies. MGN alone did not alter the proliferation index. Irradiation caused a dose-dependent decline in the proliferation index, while treatment of HPBLs with 50 ,/ml MGN significantly elevated the proliferation index in irradiated cells. MGN treatment reduced hydrogen peroxide-induced lipid peroxidation in HPBLs in a concentration-dependent fashion. In cell-free studies, MGN inhibited the induction of ·OH (hydroxyl), O2·, (superoxide), DPPH (1,1-diphenyl-2-picrylhydrazyl), and ABTS·+ (2,2-azino-bis-3-ethyl benzothiazoline-6-sulphonic acid) radicals in a dose-dependent manner. The results of this study indicate that MGN possesses radioprotective properties by suppressing the effects of free radicals. Environ. Mol. Mutagen. 45:000,000, 2005. © 2005 Wiley-Liss, Inc. [source] Molecular relaxation and metalloenzyme active site modelingINTERNATIONAL JOURNAL OF QUANTUM CHEMISTRY, Issue 4-5 2002James W. Whittaker Abstract Metalloenzymes represent a broad class of important biomolecules containing an essential metal ion cofactor in their catalytic active sites, forming biologic metal complexes that perform a wide range of important functions: activation of small molecules (O2, N2, H2, CO), atom transfer chemistry, and the control of oxidation equivalents. The structures of many metalloenzyme active sites have been defined by X-ray crystallography, revealing transition metal ions in unique low-symmetry environments. These bioinorganic complexes present significant challenges for computational studies aimed at going beyond crystal structures to develop a detailed understanding of the catalytic mechanisms. Considerable progress has been made in the theoretical characterization of these sites in recent years, supported by the availability of efficient computational tools, in particular density functional methods. However, the ultimate success of a theoretical model depends on a number of factors independent of the specific computational method used, including the quality of the initial structural data, the identification of important environmental perturbations and constraints, and experimental validation of theoretical predictions. We explore these issues in detail and illustrate the effects of molecular relaxation in calculations of two metalloenzymes, manganese superoxide dismutase and galactose oxidase. © 2002 Wiley Periodicals, Inc. Int J Quantum Chem, 2002 [source] Surface-enhanced Raman sensors: early history and the development of sensors for quantitative biowarfare agent and glucose detectionJOURNAL OF RAMAN SPECTROSCOPY, Issue 6-7 2005Christy L. Haynes Abstract Surface-enhanced Raman spectroscopy (SERS) is a powerful technique for the sensitive and selective detection of low-concentration analytes. This paper includes a discussion of the early history of SERS, the concepts that must be appreciated to optimize the intensity of SERS and the development of SERS-based sensors. In order to achieve the lowest limits of detection, both the relationship between surface nanostructure and laser excitation wavelength, as well as the analyte/surface binding chemistry, must be carefully optimized. This work exploits the highly tunable nature of nanoparticle optical properties to establish the first set of optimization conditions. The SERS enhancement factor, EFSERS, is optimized when the energy of the localized surface plasmon resonance (LSPR) lies between the energy of the excitation wavelength and the energy of the vibrational band of interest. With the narrow LSPRs used in this work, it is straightforward to achieve EFSERS , 108. These optimization conditions were exploited to develop SERS-based sensors for two important target molecules: a Bacillus anthracis biomarker and glucose in a serum protein mixture. Using these optimized film-over-nanosphere surfaces, an inexpensive, portable Raman spectrometer was used successfully to detect the infectious dose of Bacillus subtilis spores with only a 5-s data collection. The biomarker used to detect the Bacillus subtilis spores binds irreversibly to SERS substrates, whereas other important biomolecules, such as glucose, do not have any measurable binding affinity to a bare silver surface. To overcome this difficulty, a biocompatible partition layer was self-assembled on the SERS substrate before exposure to the analyte solution. Using the partition layer approach to concentrate glucose near the SERS-active substrate, physiological glucose concentrations can be detected even in the presence of interfering serum proteins. Copyright © 2005 John Wiley & Sons, Ltd. [source] The structure of a family GH25 lysozyme from Aspergillus fumigatusACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 9 2010Justyna E. Korczynska Lysins are important biomolecules which cleave the bacterial cell-wall polymer peptidoglycan. They are finding increasing commercial and medical application. In order to gain an insight into the mechanism by which these enzymes operate, the X-ray structure of a CAZy family GH25 `lysozyme' from Aspergillus fumigatus was determined. This is the first fungal structure from the family and reveals a modified ,/,-barrel-like fold in which an eight-stranded ,-barrel is flanked by three ,-helices. The active site lies toward the bottom of a negatively charged pocket and its layout has much in common with other solved members of the GH25 and related GH families. A conserved active-site DXE motif may be implicated in catalysis, lending further weight to the argument that this glycoside hydrolase family operates via a `substrate-assisted' catalytic mechanism. [source] | ||||||||||