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Fucosylated alpha-fetoprotein (AFP-L3) is a more specific and sensitive biomarker for early diagnosis of hepatocellular carcinoma (HCC) than only the alpha-fetoprotein (AFP) level. Rapid and simple detection of AFP-L3 level greatly facilitates the early detection as well as the treatment of HCC, resulting in the reduction of mortality. Here, we developed a rapid and sensitive lateral flow assay (LFA) using lectin Lens culinaris agglutinin (LCA), which has a specific affinity to AFP-L3 fraction of AFP, as a biorecognition element for determination of the fucosylation of AFP. The assay is based on a sandwich format performed on a lateral flow test strip. LCA was immobilized on the membrane as a test line (T). Quantitative detection of AFP-L3 was achieved by measuring the green color intensity of captured gold nanoparticle conjugates on the T and control line (C) utilizing an in-house test strip reader. The calculated absorbance obtained by the green color intensity signals proportionally increased with AFP concentrations. The developed lectin-based LFA provided a detection limit of 0.8 ng/mL for AFP with a linear range between 1.5 and 160.0 ng/mL within an assay time of 10 min. Recoveries between 74.5% and 113.2% with relative standard deviations of 5.2%-8.7% for measuring spiked human serum were also achieved. The results reveal that the proposed assay offers a rapid, sensitive, and specific method, which is useful for development in point-of-care testing for early detection and treatment of HCC., (© 2023 Wiley Periodicals LLC.)

This work aims to develop a more robust, easy-to-use, low-pressure, and cost-effective nonsuppressed open tubular capillary ion chromatography (NS-OTIC) approach with online dialysis for small ions determination in drinks. The fabricated device was applied for two selected columns, including poly(butadiene-maleic acid) on a 50-μm bore and AS18 Latex on 25-µm bore fused silica capillaries, for the separation of mixed cations (Na + , K + , Ca 2+ , Mg 2+ ) and mixed anions (Cl - , Br - , NO 2 - , NO 3 - ), respectively. High concentrations of ions (up to 100 mM) level can be directly introduced into the NS-OTIC system without an off-line (manual) dilution step. The linear relationship of the peak area and concentration of model ions can be obtained with a resolution > 1.1. The repeatability of the peak area for both OTIC columns was < 6% RSD. Juice and tea samples were successfully analyzed with % recoveries of 77-112 and 90-119 for cation and anion determinations, respectively., (Copyright © 2022 Elsevier Ltd. All rights reserved.)

A microfluidic hydrodynamic sequential injection (μHSI) spectrophotometric system was designed and fabricated. The system was built by laser engraving a manifold pattern on an acrylic block and sealing with another flat acrylic plate to form a microfluidic channel platform. The platform was incorporated with small solenoid valves to obtain a portable setup for programmable control of the liquid flow into the channel according to the HSI principle. The system was demonstrated for the determination of phosphate using a molybdenum blue method. An ascorbic acid, standard or sample, and acidic molybdate solutions were sequentially aspirated to fill the channel forming a stack zone before flowing to the detector. Under the optimum condition, a linear calibration graph in the range of 0.1-6mg P L -1 was obtained. The detection limit was 0.1mgL -1 . The system is compact (5.0mm thick, 80mm wide × 140mm long), durable, portable, cost-effective, and consumes little amount of chemicals (83μL each of molybdate and ascorbic acid, 133μL of the sample solution and 1.7mL of water carrier/run). It was applied for the determination of phosphate content in extracted soil samples. The percent recoveries of the analysis were obtained in the range of 91.2-107.3. The results obtained agreed well with those of the batch spectrophotometric method., (Copyright © 2017 Elsevier B.V. All rights reserved.)

This review article is an update of our previous one by C. Puangpila, E. Mayadunne, and Z. El Rassi, Electrophoresis 2015, 36, 238-252. Similarly to the previous article, this review has two main topics, including (i) proteomic sample preparation (e.g., depletion of high-abundance proteins, reduction of the protein dynamic concentration range, and enrichment of a particular subproteome), and (ii) the subsequent chromatographic and/or electrophoretic prefractionation prior to protein separation and identification by LC-MS/MS. More than 70 papers published in the period extending from mid-2014 to the present have been reviewed. Although an effort was made to yield a comprehensive review article, one may safely state that this review article is by no means thorough, and the aim was to rather provide a concise description of the latest developments in the field., (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

This research reports a proof-of-concept that describes an instrumental approach that is gel free and label free at both the separation and mass spectrometry ends for the capturing and identification of differentially expressed proteins (DEPs) in diseases, e.g., cancers. The research consists of subjecting/processing equalized and non-equalized (i.e., untreated) disease-free and hepatocellular carcinoma (HCC) human sera via a multicolumn platform for capturing/fractionating human serum fucome. The equalization was performed via the combinatorial peptide ligand library (CPLL) beads technology that ensured narrowing the protein concentration range, thus allowing the detection of low abundance proteins. The equalized and non-equalized disease-free and HCC sera were first fractionated online onto two lectin columns specific to fucose, namely Aleuria aurantia lectin (AAL) and Lotus tetragonolobus agglutinin (LTA) followed by the online fractionation of the lectin captured fucome by reversed phase chromatography. The online desalted fractions were first subjected to trypsinolysis and then to liquid chromatography-mass spectrometry (LC-MS/MS) analysis. In comparison with untreated serum, the CPLL treated serum is superior in terms of the total number of identified DEPs, which reflected an increased number of DEPs in a wide abundance range. The DEPs in HCC serum were found to be 70 and 40 in both LTA and AAL fractions for the serum treated by CPLL and untreated serum, respectively. In addition, the platform combined with the CPLL treatment was accomplished with virtually no sample loss and dilution as well as with no experimental biases and sample labeling when comparing the diseased-free and cancer sera using LC-MS/MS., (Copyright © 2015 Elsevier B.V. All rights reserved.)

This review article expands on the previous one (S. Selvaraju and Z. El Rassi, Electrophoresis 2012, 33, 74-88) by reviewing pertinent literature in the period extending from early 2011 to present. As the previous review article, the present one is concerned with proteomic sample preparation (e.g., depletion of high-abundance proteins, reduction of the protein dynamic concentration range, enrichment of a particular subproteome), and the subsequent chromatographic and/or electrophoretic prefractionation prior to peptide separation and identification by LC-MS/MS. This review article, however, is distinguished from its earlier version by expanding on capturing/enriching subphosphoproteomes by immobilized metal affinity chromatography and metal oxide affinity chromatography. Seventy-seven papers published in the period extending from mid-2011 to the present have been reviewed. By no means this review article is exhaustive, given the fact that its aim is to give a concise treatment of the latest developments in the field., (© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Two different neutral nonpolar monolithic columns series (designated as A and B columns series) each consisting of three columns at varying n-alkyl chain length were prepared by the copolymerization of the functional monomers C8-methacrylate, C12-acrylate, or C16-methacrylate with the cross-linking monomer pentaerythritol triacrylate (PETA) to yield monoliths with surface bound C8, C12, and C16 chains. In the A columns series, the composition of the functional monomers and crosslinker was adjusted to yield comparable chromatographic retention regardless of the alkyl chain length. In the B columns series, the composition of the functional monomers and crosslinker was kept constant yielding chromatographic retention, which increased as expected in the order of increasing the n-alkyl chain length. Due to their direct influences on the monolith porosity and retention energetic, the nature and composition of the monomers at a given porogen composition have largely affected the solute's mass transfer characteristics and sorption kinetics, as assessed by the van Deemter plots and separation efficiencies. The C16-monolith of the A series yielded the highest separation efficiency toward small solutes, but the A columns series were inadequate for protein separation. The C8-monolith of the B series provided the best separation efficiency for proteins while for tryptic peptide mapping, the C16-monolith of the A series seems to provide the best separation. For large protein molecules, the energetically "softer" C8 surface allowed faster sorption kinetics and in turn improved efficiency, while an energetically "harder" C16 surface favored better separation of the smaller size peptide solutes., (© 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Equations and theoretical models for MEKC separation selectivity (α(MEKC) ) were established to explain a change in separation and electrophoretic mobility order of fully charged analytes, in which α(MEKC) is related to the dimensionless values of mobility selectivity in CZE (α(CZE)) and retention selectivity (α(k)) in MEKC, and where α(CZE) and α(k) are defined as the ratio of electrophoretic mobility in CZE and the ratio of retention factor (k) in MEKC for two charged analytes, respectively. Using four alkylparabens as test analytes, excellent agreement was found between the observed α(MEKC) and the proposed α(MEKC) models of test analytes in MEKC over a wide range of SDS concentrations and values of k. For example, in comparison with CZE separation of charged analytes, MEKC separation can enhance separation selectivity up to the maximum value when the selectivity ratio (ρ) is greater than 1.0 (ρ=α(k)/α(CZE)), while lower separation selectivity is obtained with ρ<1.0 (α(CZE) >α(k) >1)., (Copyright © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)