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Characterization of Phyto-Constituents
Published in Rohit Dutt, Anil K. Sharma, Raj K. Keservani, Vandana Garg, Promising Drug Molecules of Natural Origin, 2020
Himangini, Faizana Fayaz, Anjali
In the early 1980s, capillary electrophoresis (CE) was developed as a powerful analytical and separation device. It detects the purity/complexity of a sample and can deal with every kind of charged components of sample from simple inorganic ions to DNA. Thusly, the utilization of fine electrophoretic techniques expanded in the investigation of natural drugs in last past years. The working of CE examination can be performed by electric field worked in tight cylinders which prompts division of numerous mixes. The separation of different charged components caused due to applied voltage in between buffer filled capillaries which generates the production of ions depending on their mass and charge ratio. Frequently used electrophoresis techniques are capillary zone electrophoresis (CZE), capillary gel electrophoresis (CGE), and capillary isoelectric focusing (CIEF). CE is the most proficient strategy utilized for the division and investigation of modest number of analytes with excellent partition capacity. In the meantime it has comparative specialized qualities as that of liquid chromatography; anyway it is a superior technique for building up the chemical fingerprints of the natural medications.
Synthesis of Bioactive Peptides for Pharmaceutical Applications
Published in Peter Grunwald, Pharmaceutical Biocatalysis, 2019
Jaison Jeevanandam, Ashish Kumar Solanki, Shailza Sharma, Prabir Kumar Kulabhusan, Sapna Pahil, Michael K. Danquah
Capillary electrophoresis has also been used for biopeptide separation which separates analytes based on its charge in solution. Numerous separation modes are present in CE which includes capillary isoelectric focusing, capillary zone electrophoresis and micellar electro-kinetic capillary chromatography. Though RP-HPLC is the most favored separation approach for biopeptides, the rapid investigation time, low consumption of sample and reagent, wide detection schemes including fluorescence, UV, ESI-MS and versatile separation mode makes CE an influential alternative to HPLC (Black et al., 2015).
Fingerprinting Techniques for Herbal Drugs Standardization
Published in Ravindra Kumar Pandey, Shiv Shankar Shukla, Amber Vyas, Vishal Jain, Parag Jain, Shailendra Saraf, Fingerprinting Analysis and Quality Control Methods of Herbal Medicines, 2018
Ravindra Kumar Pandey, Shiv Shankar Shukla, Amber Vyas, Vishal Jain, Parag Jain, Shailendra Saraf
Capillary electrophoresis (CE) was introduced in the early 1980s as a powerful analytical and separation technique and has since been developed almost explosively. It allows an efficient way to document the purity/complexity of a sample and can handle virtually every kind of charged sample components ranging from simple inorganic ions to DNA. Thus, there has been an obvious increase of electrophoretic methods, especially capillary electrophoresis, used in the analysis of herbal medicines in the last decades. The more or less explosive development of capillary electrophoresis since its introduction has to a great extent paralleled that of liquid chromatography. The techniques most often used are capillary zone electrophoresis (CZE), capillary gel electrophoresis (CGE), and capillary isoelectric focusing (CIEF). CE is promising for the separation and analysis of active ingredients in herbal medicines, since it needs only small amounts of standards and can analyze samples rapidly with very good separation ability. Also, it is a good tool for producing the chemical fingerprints of the herbal medicines, since it has similar technical characteristics as liquid chromatography. Recently, several studies dealing with herbal medicines have been reported and two kinds of medicinal compounds, that is, alkaloids and flavonoids, have been studied extensively (Yang and Smetena, 1995).
Analytical techniques for multiplex analysis of protein biomarkers
Published in Expert Review of Proteomics, 2020
Alain Van Gool, Fernado Corrales, Mirjana Čolović, Danijela Krstić, Begona Oliver-Martos, Eva Martínez-Cáceres, Ivone Jakasa, Goran Gajski, Virginie Brun, Kyriacos Kyriacou, Izabela Burzynska-Pedziwiatr, Lucyna Alicja Wozniak, Stephan Nierkens, César Pascual García, Jaroslav Katrlik, Zanka Bojic-Trbojevic, Jan Vacek, Alicia Llorente, Felicia Antohe, Viorel Suica, Guillaume Suarez, Ruben t’Kindt, Petra Martin, Deborah Penque, Ines Lanca Martins, Ede Bodoki, Bogdan-Cezar Iacob, Eda Celikbas, Suna Timur, John Allinson, Christopher Sutton, Theo Luider, Saara Wittfooth, Marei Sammar
Capillary electrophoresis (CE) is a collective term representing a number of electrokinetic separation techniques performed in narrow bore capillaries or microchips. Capillary zone electrophoresis (CZE) is widely used for the separation of charged species based on differences in their charge density. CE offers an outstanding separation efficiency for peptides and small proteins, being complementary with liquid chromatographic (LC) separations, both in ‘top-down’ and ‘bottom-up’ proteomics. Interfacing CE to MS has matured into a robust clinical investigational tool in several disease areas [120], offering fast separations with good analytical sensitivities in protein biomarker analysis [121]. The most popular interface of CZE-MS coupling is via electrospray ionization (ESI). Both sheath-flow and sheath-less interface designs are employed. To circumvent significant sheath liquid-mediated sample dilution and the limited sample loading capacity of CE, tapered emitters operating in the nanospray regime not only support lower flow rates of the sheath liquid, but also contribute to better desolvation, enhanced sensitivity, and better salt tolerance [122]. Miniaturization to a single microchip (MCE) with the use of an electrophoretic step prior to biomarker detection may lead to an attractive clinical diagnostic tool [123].
Proteomics for cancer drug design
Published in Expert Review of Proteomics, 2019
Amanda Haymond, Justin B. Davis, Virginia Espina
Generally, methods for determining protein structure, function, and formulation purity are well established. Primary structure is often determined by mass spectrometry-based peptide mapping, intact mass analysis, sequence coverage analysis, and N-terminal or C-terminal sequencing [112,113]. Higher order structure can be evaluated by Fourier transform infrared spectroscopy, differential scanning calorimetry, circular dichroism spectroscopy, free thiol analysis, and disulfide bond analysis [103,104]. Charge is evaluated by capillary zone electrophoresis, isoelectric focusing, and ion exchange chromatography. Aggregation is analyzed via gel and liquid based chromatography. Affinities are determined via ELISA and SPR [112,113].
Reference interval transference of common clinical biomarkers
Published in Scandinavian Journal of Clinical and Laboratory Investigation, 2021
Panyang Xu, Qi Zhou, Jiancheng Xu
The difference in methodology may also be the reason for the difference in the final measured values, resulting in a weak correlation between measurement systems. For ASO assays, Abbott Architect uses the Rantz–Randall (hemolytic) method, a semiquantitative measurement of the inhibition of Streptolysin-O-induced hemolysis of erythrocytes by ASO [8]. In contrast, Roche platforms use an immunoturbidimetric assay . The results obtained using Roche assays were approximately 30% and 60% higher for the 1 to ＜6 and 6 to ＜19 year age partitions, respectively, compared to values obtained with the Abbott assay [8]. Another CALIPER transference study between Abbott and the Beckman Coulter DxC 800 also found a notable difference between the ASO assays [12]. The Mg assay, however, likely failed to transfer due to methodology differences. The Roche method is a dye binding assay, whereas the Abbott method is an enzymatic assay [34]. Serum albumin is usually measured with a dye‐binding assay, such as the bromocresol green (BCG) and bromocresol purple (BCP) methods. Researchers aimed to examine differences among albumin measurements quantified using the BCG method via the ADVIA 2400 instrument and albumin measurement quantified using the BCP method via the Dimension RxL instrument from 165 serum samples [35]. Final results show that albumin results from the BCP and BCG methods may result in unacceptable differences and clinical confusion, especially at lower albumin concentrations. Due to the influence of acute phase globulin, the concentration of albumin in the BCG method is increased, especially when the concentration is low. BCP is more specific than BCG. A superior method would be capillary zone electrophoresis. However, this assay is not without problems. Unlike BCG, the BCP method underestimates the albumin concentrations in the serum of patients with renal insufficiency. Similarly, it has been described that the BCP method underestimates albumin concentrations in patients undergoing hemodialysis. The interfering substance has not been clearly identified [35]. It is worth noting that different reagents/dyes used in the measurement process also indirectly cause methodological differences. Both Abbott and Roche measure the concentration of total calcium using colorimetric assays. However, the two methods use different dyes. Abbott Architect uses arsenazo III dye binding [36], while the Roche Modular-P method uses 5-nitro-5′-methyl-BAPTA [8].