The aggregation of proteins into insoluble amyloid fibrils coincides with the onset of numerous diseases. An array of techniques is available to study the different stages of the amyloid aggregation process. Recently, emphasis has been placed upon the analysis of oligomeric amyloid species, which have been hypothesized to play a key role in disease progression. This paper reviews techniques utilized to study aggregation of the amyloid-β protein (Aβ) associated with Alzheimer’s disease. In particular, the review focuses on techniques that provide information about the size or quantity of oligomeric Aβ species formed during the early stages of aggregation, including native-PAGE, SDS-PAGE, Western blotting, capillary electrophoresis, mass spectrometry, fluorescence correlation spectroscopy, light scattering, size exclusion chromatography, centrifugation, enzyme-linked immunosorbent assay, and dot blotting.

Wafer-enhanced electrodeionization (WE-EDI) is an electrically driven separations technology that occurs under the influence of an applied electric field and heavily depends on ion exchange resin chemistry. Unlike filtration processes, WE-EDI can be used to selectively remove ions even from high concentration systems. Because every excess ion transported increases the operating costs, the selective separation offered by WE-EDI can provide a more energy-efficient and cost-effective process, especially for highly concentrated salt solutions. This work reports the performance comparison of four commonly used cation exchange resins (Amberlite IR120 Na⁺, Amberlite IRP 69, Dowex MAC 3 H⁺, and Amberlite CG 50) and their influence on the current efficiency and selectivity for the removal of cations from a highly concentrated salt stream. The current efficiencies were high for all the resin types studied. Results also revealed that weak cation exchange resins favor the transport of the monovalent ion (Na⁺) while strong cation exchange resins either had no strong preference or preferred to transport the divalent ions (Ca²⁺ and Mg²⁺). Moreover, the strong cation exchange resins in powder form generally performed better in wafers than those in the bead form for the selective removal of divalent ions (selectivity > 1). To further understand the impact of particle size, resins in the bead form were ground into a powder. After grinding the strong cation resins displayed similar behavior (more consistent current efficiency and preference for transporting divalent ions) to the strong cation resins in powder form. This indicates the importance of resin size in the performance of wafers.

Early stages of insulin aggregation, which involve the transient formation of oligomeric aggregates, are an important aspect in the progression of Type II diabetes and in the quality control of pharmaceutical insulin production. This study is the first to utilize capillary electrophoresis (CE) with ultraviolet (UV) detection to monitor insulin oligomer formation at pH 8.0 and physiological ionic strength. The lag time to formation of the first detected species in the aggregation process was evaluated by UV-CE and thioflavin T (ThT) binding for salt concentrations from 100 mM to 250 mM. UV-CE had a significantly shorter (5–8 h) lag time than ThT binding (15–19 h). In addition, the lag time to detection of the first aggregated species via UV-CE was unaffected by salt concentration, while a trend toward an increased lag time with increased salt concentration was observed with ThT binding. This result indicates that solution ionic strength impacts early stages of aggregation and β-sheet aggregate formation differently. To observe whether CE may be applied for the analysis of biological samples containing low insulin concentrations, the limit of detection using UV and laser induced fluorescence (LIF) detection modes was determined. The limit of detection using LIF-CE, 48.4 pM, was lower than the physiological insulin concentration, verifying the utility of this technique for monitoring biological samples. LIF-CE was subsequently used to analyze the time course for fluorescein isothiocyanate (FITC)-labeled insulin oligomer formation. This study is the first to report that the FITC label prevented incorporation of insulin into oligomers, cautioning against the use of this fluorescent label as a tag for following early stages of insulin aggregation.

Here we describe DNA sample preparation methods that allow the rapid, simultaneous generation of both single-stranded conformational polymorphism (SSCP) and heteroduplex DNA elements from a single ...

Microalgae have been extensively tested for their ability to create bio-based fuels. Microalgae have also been explored as an alternative wastewater treatment solution due to their significant uptake of nitrogen and phosphorus, as well as their ability to grow in different water types. Recently, there has been significant interest in combining these two characteristics to create economic and environmentally friendly biofuel using wastewater. This study examined the growth and lipid production of the microalgae Porphyridium (P.) cruentum grown in swine wastewater (ultra-filtered and raw) as compared with control media (L⁻¹, modified f/2) at two different salt concentrations (seawater and saltwater). The cultivation of P. cruentum in the treated swine wastewater media (seawater = 5.18 ± 2.3 mgL⁻¹day⁻¹, saltwater = 3.32 ± 1.93 mgL⁻¹day⁻¹) resulted in a statistically similar biomass productivity compared to the control medium (seawater = 2.61 ± 2.47 mgL⁻¹day⁻¹, saltwater = 6.53 ± 0.81 mgL⁻¹day⁻¹) at the corresponding salt concentration. Furthermore, no major differences between the fatty acid compositions of microalgae in the treated swine wastewater medium and the control medium were observed. For all conditions, saturated acids were present in the highest amounts (≥67%), followed by polyunsaturated (≤22%) and finally monounsaturated (≤12%). This is the first study to find that P. cruentum could be used to remediate wastewater and then be turned into fuel by using swine wastewater with a similar productivity to the microalgae grown in control media.