Phosphorylated Tau at T181 accumulates in the serum of hibernating Syrian hamsters and rapidly disappears after arousal.

The search for biomarkers for the early diagnosis of neurodegenerative diseases is a growing area. Numerous investigations are exploring minimally invasive and cost-effective biomarkers, with the detection of phosphorylated Tau (pTau) protein emerging as one of the most promising fields. pTau is the main component of the paired helical filaments found in the brains of Alzheimer's disease cases and serves as a precursor in the formation of neurofibrillary tangles (NFTs). Recent research has revealed that analysis of p-Tau181, p-Tau217 and p-Tau231 in blood may be an option for detecting the preclinical stage of Alzheimer's disease. In this study, we have analyzed the values of pTau 181 in the serum of Syrian hamsters during hibernation. Naturally, over the course of hibernation, these animals exhibit a reversible accumulation of pTau in the brain tissue, which rapidly disappears upon awakening. A biosensing system based on the interferometric optical detection method was used to measure the concentration of pTau181 protein in serum samples from Syrian hamsters. This method eliminates the matrix effect and amplifies the signal obtained by using silicon dioxide nanoparticles (SiO2 NPs) biofunctionalized with the αpTau181 antibody. Our results indicate a substantial increase in the serum concentration of pTau in threonine-181 during hibernation, which disappears completely 2-3 h after awakening. Investigating the mechanism by which pTau protein appears in the blood non-pathologically may enhance current diagnostic techniques. Furthermore, since this process is reversible, and no tangles are detected in the brains of hibernating hamsters, additional analysis may contribute to the discovery of improved biomarkers. Additionally, exploring drugs targeting pTau to prevent the formation of tangles or studying the outcomes of any pTau-targeted treatment could be valuable.

Reports on the sensitivity enhancement in interferometric based biosensors by biotin-streptavidin system.

Antibody biotinylation is a process of attaching biotin molecules to antibodies by chemically modifying specific functional groups on the antibodies without altering their antigen recognition specificity. Biotin, a small vitamin, forms a strong and specific interaction with the protein streptavidin, resulting in a stable biotin-streptavidin (biotin-STV) complex. This biotin-STV interaction is widely exploited in various biotechnological applications, including biosensors. Biosensors are analytical devices that employ biological recognition elements, such as antibodies, enzymes, or nucleic acids, to detect and quantify target analytes in a sample. Antibodies are commonly used as recognition elements in biosensors due to their high specificity and affinity. In this study, the antibody anti-Bovine Serum Albumin (αBSA) has been biotinylated at different antibody:biotin ratios, and the stability of this labeling over time has been investigated. Furthermore, the sensitivity of the biosensor for detecting the Bovine Serum Albumin (BSA) protein has been compared using the biotinylated antibody and the non-biotinylated form, showing a four-fold improvement in detection. This system was also compared with the Enzyme-Linked ImmunoSorbent Assay (ELISA) technique. The advantages of using biotinylated antibodies in biosensors include increased stability and reproducibility of the biorecognition layer, as well as flexibility in sensor design, as different biotinylated antibodies can be utilized for diverse target analytes without altering the sensor's architecture.

Developing an Optical Interferometric Detection Method based biosensor for detecting specific SARS-CoV-2 immunoglobulins in Serum and Saliva, and their corresponding ELISA correlation.

The standard rapid approach for the diagnosis of coronavirus disease 2019 (COVID-19) is the detection of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) RNA. The detection of specific anti-SARS-CoV-2 immunoglobulins is crucial for screening people who have been exposed to the virus, whether or not they presented symptoms. Recent publications report different methods for the detection of specific IgGs, IgMs, and IgAs against SARS-CoV-2; these methods mainly detect immunoglobulins in the serum using conventional techniques such as rapid lateral flow tests or enzyme-linked immunosorbent assay (ELISA). In this article, we report the production of recombinant SARS-CoV-2 spike protein and the development of a rapid, reliable, cost-effective test, capable of detecting immunoglobulins in serum and saliva samples. This method is based on interferometric optical detection. The results obtained using this method and those obtained using ELISA were compared. Owing to its low cost and simplicity, this test can be used periodically for the early detection, surveillance, detection of immunity, and control of the spread of COVID-19.