V. Bório, Rubens Vinha, R. Nicolau, H. P. M. D. Oliveira, C. J. Lima, L. Silveira
{"title":"Quantitative Evaluation of Acetaminophen in Oral Solutions by Dispersive Raman Spectroscopy for Quality Control","authors":"V. Bório, Rubens Vinha, R. Nicolau, H. P. M. D. Oliveira, C. J. Lima, L. Silveira","doi":"10.1155/2012/108041","DOIUrl":"https://doi.org/10.1155/2012/108041","url":null,"abstract":"This work used dispersive Raman spectroscopy to evaluate acetaminophen in commercially available formulations as an analytical methodology for quality control in the pharmaceutical industry. Raman spectra were collected using a near-infrared dispersive Raman spectrometer (830 nm, 50 mW, 20 s exposure time) coupled to a fiber optic probe. Solutions of acetaminophen diluted in excipient (70 to 120% of the commercial concentration of 200 mg/mL) were used to develop a calibration model based on partial least squares (PLSs) applied to Raman spectra of solutions and, subsequently, obtain linearity, accuracy, precision (repeatability), and sensitivity of the method using the near-infrared spectroscopy (NIRS) as a gold standard method. This model was used to predict the acetaminophen concentration in commercial samples from different lots of acetaminophen formulations (200 mg/mL) with a PLS-prediction error of about 0.6%. Commercial medicines had PLS predicted concentrations errors below 2.5%, whereas NIRS had an error of about 3.7% compared to the label concentration. It has been demonstrated the applicability of Raman spectroscopy with fiber probe for quality control in pharmaceutical industry of commercial formulations.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"1 1","pages":"215-228"},"PeriodicalIF":0.0,"publicationDate":"2012-06-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"79218496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Role of Vibrational Spectroscopy in Stem Cell Research","authors":"C. Aksoy, F. Severcan","doi":"10.1155/2012/513286","DOIUrl":"https://doi.org/10.1155/2012/513286","url":null,"abstract":"Recent researches have mainly displayed the significant role of stem cells in tissue renewal and homeostasis with their unique capacity to develop different cell types. These findings have clarified the importance of stem cells to improve the effectiveness of any cell therapy for regenerative medicine. Identification of purity and differentiation stages of stem cells are the greatest challenges of stem cell biology and regenerative medicine. The existing methods to carefully monitor and characterize the stem cells have some unwanted effects on the properties of stem cells, and these methods also do not provide real-time information about cellular conditions. These challenges enforce the usage of nondestructive, rapid, sensitive, high quality, label-free, cheep, and innovative chemical monitoring methods. In this context, vibrational spectroscopy provides promissing alternative to get new information into the field of stem cell biology for chemical analysis, quantification, and imaging of stem cells. Raman and infrared spectroscopy and imaging can be used as a new complimentary spectroscopic approaches to gain new insight into stem cell reseaches for future therapeutic and regenerative medicines. In this paper, recent developments in applications of vibrational spectroscopy techniques for stem cell characterization and identification are presented.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"25 1","pages":"167-184"},"PeriodicalIF":0.0,"publicationDate":"2012-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81667242","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Lei Huang, Lianzhi Li, Haili Li, Chaohui Gao, Hui Cui, Xiangshi Tan
{"title":"Multispectroscopic Study of the Interaction of Chloramphenicol with Human Neuroglobin","authors":"Lei Huang, Lianzhi Li, Haili Li, Chaohui Gao, Hui Cui, Xiangshi Tan","doi":"10.1155/2012/192591","DOIUrl":"https://doi.org/10.1155/2012/192591","url":null,"abstract":"The interaction between chloramphenicol (CHL) and neuroglobin (Ngb) has been investigated by using fluorescence, synchronous fluorescence, UV-Vis and circular dichroism (CD) spectroscopy. It has been found that CHL molecule can quench the intrinsic fluorescence of Ngb in a way of dynamic quenching mechanism, which was supported by UV-Vis spectral data. Their effective quenching constants (𝐾SV) are 2.2×104, 2.6×104, and3.1×104 L·mol−1 at 298 K, 303 K, and 308 K, respectively. The enthalpy change (Δ𝐻) and entropy change (Δ𝑆) for this reaction are 26.42 kJ·mol−1 and 171.7 J·K−1, respectively. It means that the hydrophobic interaction is the main intermolecular force of the interaction between CHL and Ngb. Synchronous fluorescence spectra showed that the microenvironment of tryptophan and tyrosine residues of Ngb has been changed slightly. The fluorescence quenching efficiency of CHL to tyrosine residues is a little bit more than that to tryptophan residues of Ngb. Furthermore, CD spectra indicated that CHL can induce the formation of α-helix of Ngb.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"13 1","pages":"143-154"},"PeriodicalIF":0.0,"publicationDate":"2012-06-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86964505","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Determination of Collagen Fibers Arrangement in Bone Tissue by Using Transformations of Raman Spectra Maps","authors":"T. Buchwald, M. Kozielski, M. Szybowicz","doi":"10.1155/2012/261487","DOIUrl":"https://doi.org/10.1155/2012/261487","url":null,"abstract":"The goal of this work was to evaluate the ability of Raman spectroscopy to identify molecular organization and chemical composition of extracellular matrix such as the collagen fibers arrangement, the level of mineralization, and the carbonate accumulation in mineral phase in spongy bone of the human head of the femur. Changes in composition and structure of the spongy bone tissue were illustrated using maps of polarized Raman spectra. In particular, the purpose of the present study was determination of arrangement of mineralized collagen on surface of trabecula by using transformations of Raman spectra maps. Transformations of Raman spectra maps were needed in order to remove impact of chemical composition on images of Raman spectra map, which display the collagen fibers orientation. These transformations allow to obtain simultaneously the distribution of constituents of bone and arrangement of collagen fibers on tissue surface. A method to indicate the collagen orientations is developed to understand the molecular organization in healthy and unhealthy bone at the microstructural level.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"75 1","pages":"107-117"},"PeriodicalIF":0.0,"publicationDate":"2012-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76404601","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Marc Grosserueschkamp, C. Nowak, W. Knoll, R. Naumann
{"title":"Time-resolved surface-enhanced resonance Raman spectro-electrochemistry of heme proteins","authors":"Marc Grosserueschkamp, C. Nowak, W. Knoll, R. Naumann","doi":"10.3233/SPE-2010-0414","DOIUrl":"https://doi.org/10.3233/SPE-2010-0414","url":null,"abstract":"Heme proteins such as cytochrome c (cc) play a fundamental role in many biological processes. Surface-enhanced resonance Raman spectroscopy (SERRS) combined with electrochemical methods is an ideal tool to study the redox processes of heme proteins. In this context we designed a new measuring cell allowing for simultaneous electrochemical manipulation and high sensitive SERRS measurements of heme proteins. The measuring cell is based on an inverted rotating disc electrode for excitation by using a confocal Raman microscope. Furthermore, we developed a SER(R)S-active silver modified silver substrate for spectro-electrochemical applications. For this purpose silver nanoparticles (AgNPs) were adsorbed on top of a planar silver surface. The substrate was optimized for an excitation wavelength of 413 nm corresponding to the resonance frequency of heme structures. An enhancement factor of 10 5 was achieved. The high performance of the new measuring cell in combination with","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"82 1","pages":"125-129"},"PeriodicalIF":0.0,"publicationDate":"2010-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74180489","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Magnetization‒transfer 31P NMR of biochemical exchange in vivo: Application to creatine kinase kinetics","authors":"H. Möller, D. Wiedermann","doi":"10.1155/2002/326454","DOIUrl":"https://doi.org/10.1155/2002/326454","url":null,"abstract":"Phosphorus‒31 saturation‒transfer NMR spectroscopy provides an elegant means to study fluxes through the creatine kinase reaction in human skeletal muscle. To obtain reliable quantitative kinetic information, experimental imperfections, such as incomplete saturation and radiofrequency bleed over need to be addressed appropriately. In resting muscle, creatine kinase was near equilibrium both in normal controls and in a patient with impaired oxidative phosphorylation. Oral intake of high doses of creatine monohydrate for several days resulted in significantly increased concentrations of phosphocreatine but had no measurable effect on the phosphocreatine resynthesis rate in resting muscle.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"4 1","pages":"207-216"},"PeriodicalIF":0.0,"publicationDate":"2002-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73133695","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
R. Dieden, D. Latinne, C. Baldari, Nicoletta Maton, A. Aubry, R. Verbeeck, M. Zurini, G. Lhoëst
{"title":"Cyclization reactions of IMM-125 and oxidation of cyclosporin A amino-acid 1 in the alpha position of the double bond lead to the loss of in vitro immunosuppressive activity","authors":"R. Dieden, D. Latinne, C. Baldari, Nicoletta Maton, A. Aubry, R. Verbeeck, M. Zurini, G. Lhoëst","doi":"10.1155/2000/491283","DOIUrl":"https://doi.org/10.1155/2000/491283","url":null,"abstract":"Cyclosporin A (CsA) and IMM-125, a hydroxyethyl derivative of D-serine CsA, are cyclic undecapeptides of molecular weight 1201.8 and 1261.8, respectively. The main metabolites still possessing the undecapeptide structure were found to be compounds resulting from the biotransformation of amino acids 4, 9 and 1. Under the influence of the hepatic cytochrome P-450-dependent monooxygenase system, CsA and IMM-125 amino acid 1 are metabolized to a mono-hydroxylated compound (metabolite M-17) and to a dihydrodiol. A metabolite M18 was found to be the result of a non-enzymic intramolecular formation of a tetrahydrofuran derivative from metabolite M17. Since the existence of a CsA dihydrodiol was reported and since epoxides are considered as the dihydrodiol precursors, the aim of the present work was to prove that the same non-enzymic intramolecular formation of a tetrahydrofuran ring could occur by nucleophilic attack of the amino-acid 1 beta -hydroxy group at the epsilon -position of the freshly formed epoxide by reaction of IMM-125 with m-chloroperbenzoic acid and cyclosporin A with selenium oxide. The immunosuppressive activity of the compounds, as measured by the mixed lymphocyte reaction and by the luciferase activity of a Jurkat-T-cell line stably transfected with the NF-AT/luc reporter plasmid, was found negligible for IMM-125 compared to the parent drug as well as for the cyclosporin A derivative. Structures of the IMM-125 and CsA derivatives were elucidated by electrospray mass-spectrometry and NMR spectroscopy.","PeriodicalId":51163,"journal":{"name":"Spectroscopy-An International Journal","volume":"1 1","pages":"215-228"},"PeriodicalIF":0.0,"publicationDate":"2000-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"74491105","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}