Aptamer-Linked Photonic Crystal Assay for High-Throughput Screening of HIV and SARS-CoV-2.

We present a microplate assay for the detection of HIV and SARS-CoV-2 which involves the preadsorption of carboxy-modified polystyrene microspheres to the microplate wells and their self-assembly leading to the formation of a photonic crystal colloidal array (PCCA). PCCA is then cross-linked with amino-modified aptamers selected for viral cell surface glycoproteins, i.e., S1-protein of SARS-CoV-2 and gp120 of the human immunodeficiency virus (HIV), to develop an aptamer-linked photonic crystal assay (ALPA). ALPA is then utilized as a proof-of-concept method for the detection of S1-protein, gp120, and two whole viruses, i.e., SARS-CoV-2 and HIV, as well. The aptamers are stable at room temperature and can bind with the viruses' proteins via hydrogen bonding. This binding leads to color generation from PCCA, and the signal can easily be measured and quantified by a UV/vis spectrometer. The assay carries the advantage of a two-step detection process by the addition of the virus sample directly to a 96-well microplate and incubation of 5 min followed by convenient detection through a UV/vis-spectrometer. The assay does not require any additional reagents and can be customized for similar viruses utilizing specific aptamers targeting their cell surface receptors.

Advances in aptamers against Aß and applications in Aß detection and regulation for Alzheimer's disease.

Alzheimer's disease (AD) is an irreversible neurodegenerative disease, causing profound social and economic implications. Early diagnosis and treatment of AD have faced great challenges due to the slow and hidden onset. ß-amyloid (Aß) protein has been considered an important biomarker and therapeutic target for AD. Therefore, non-invasive, simple, rapid and real-time detection methods for AD biomarkers are particularly favored. With the development of Aß aptamers, the specific recognition between aptamers and Aß plays a significant role in AD theranostics. On the one hand, aptamers are applied to construct biosensors for Aß detection, which provides possibilities for early diagnosis of AD. On the other hand, aptamers are used for regulating Aß aggregation process, which provides potential strategies for AD treatment. Many excellent reviews have summarized aptamers for neurodegenerative diseases or biosensors using specific recognition probes for Aß detection applications in AD. In this review, we highlight the crucial role of the design, classification and applications of aptamers on Aß detection as well as inhibition of Aß aggregation for AD.

A Parametric Study on Overband Radial Build for a REBCO 800-MHz Insert of a 1.3-GHz LTS/HTS NMR Magnet.

A high-resolution 1.3-GHz/54-mm low-temperature superconducting/high-temperature superconducting (HTS) nuclear magnetic resonance magnet (1.3 G) is currently being built at Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology. One of its key components is an 800-MHz HTS insert (H800) comprising three nested coils. Each coil is a stack of double-pancake coils wound with 6-mm-wide 75-µm-thick REBCO tape. For this H800 generating its self-field of 18.6 T and being exposed to a total field as high as 30.5 T, overbanding each pancake coil is necessary to keep the conductor strain at < 0.6%. Although electromagnetic and mechanical details of the H800 had been considered during its design stage, a parametric study on the overband radial build considering winding tension effect should further confirm the results of our previous analysis. Thus, in this paper, based on Maxwell's equations and the equilibrium equations for mechanical deformation, we examine stress levels that the H800 experiences as H800 undergoes winding-energizing sequences during operation at 1.3 GHz. We also discuss the effects of overband radial build and winding tension on conductor stress in each coil. Finally, based on this analysis, we may further optimize the stainless-steel overbanding and winding tension on each H800 coil.

[Comparison of one-step and two-step methods for pI determination of proteins and polypeptides by capillary isoelectric focusing].

One-step and two-step capillary isoelectric focusing (clEF) methods were employed the separation and pI determination of proteins and polypeptides. The parameters affecting the analysis efficiency, such as the sample solution, injection volume, focusing voltage, focusing time and driving conditions were optimized. The comparison of the two methods for separation of cytochrome C, hemoglobin, myoglobin, transferrin, bovine serum albumin and six polypeptides showed that the one-step cIEF was simple and fast, which could determine the pI of single component as well as it was rapid for protein and polypeptide separation, but it could not get good resolution or accurate pI of each component in a mixed sample. The two-step cIEF was more complex and needed longer time, however, which could separate and exactly determine the pI of each component in the mixture, and the pI value of each component determined was consistent with that determined using a single sample. The two methods are complementary, and can be widely used in rapid and accurate determination of the pI of amphiphilic biological particles.