Highly Sensitive Flow Cytometry Biosensor with a High Signal-to-Background Ratio for FEN1 Analysis via Solid-Phase Interface-Mediated Primer Exchange Reaction Amplification.

Flap endonuclease 1 (FEN1) is a specific enzyme capable of recognizing and cleaving triplex DNA structures and releasing 5'-flap fragments. It plays a crucial role in the DNA metabolism of cells, participating in DNA replication and the repair of damaged DNA. Additionally, FEN1 is overexpressed in various tumor tissues, promoting tumor progression and drug resistance through different regulatory mechanisms.

An ultra-sensitive fluorescence biosensor with rolling circle amplification and CRISPR/Cas12a one-pot system for FEN1 detection.

Flap endonuclease 1 (FEN1), a structure-specific nuclease, has been reported to be widely involved in the development of cancer, and recognized as a new biomarker for cancer. However, there remains a deficiency in the availability of simple, rapid and reliable biosensors for its detection. We have constructed a cascade signal amplification fluorescence biosensor for ultra-sensitive and rapid detection of FEN1.

Aggregation and Oligomerization Characterization of ß-Lactoglobulin Protein Using a Solid-State Nanopore Sensor.

Protein aggregation is linked to many chronic and devastating neurodegenerative human diseases and is strongly associated with aging. This work demonstrates that protein aggregation and oligomerization can be evaluated by a solid-state nanopore method at the single molecule level. A silicon nitride nanopore sensor was used to characterize both the amyloidogenic and native-state oligomerization of a model protein ß-lactoglobulin variant A (βLGa).

Mild cognitive impairment in maintenance hemodialysis patients: a cross-sectional survey and cohort study.

Introduction: Few studies focused on mild cognitive impairment (MCI) in maintenance hemodialysis (MHD) patients. This study was conducted to survey the prevalence, the potent risk factors of MCI in MHD patients, and further observe the progress of MCI in a period of 6 months.

Methodology: Mini-Mental State Examination, and Montreal Cognitive Assessment were used to assess cognitive condition.

In vitro formation of amyloid from alpha-synuclein is dominated by reactions at hydrophobic interfaces.

Most in vitro investigations of alpha-Synuclein (alphaSyn) aggregation and amyloidogenesis use agitation in the presence of air and/or Teflon to accelerate kinetics. The effect of the agitation is implicitly or explicitly attributed to mass transfer or fibril fragmentation. This paper evaluates these hypotheses by agitating alphaSyn under typical amyloidogenic conditions with controlled numbers of balls made of polytetrafluoroethylene (PTFE), polymethylmethacrylate (PMMA), and borosilicate glass with no headspace.

Role of small oligomers on the amyloidogenic aggregation free-energy landscape.

We combine atomic-force-microscopy particle-size-distribution measurements with earlier measurements on 1-anilino-8-naphthalene sulfonate, thioflavin T, and dynamic light scattering to develop a quantitative kinetic model for the aggregation of beta-lactoglobulin into amyloid. We directly compare our simulations to the population distributions provided by dynamic light scattering and atomic force microscopy. We combine species in the simulation according to structural type for comparison with fluorescence fingerprint results.

Beta-lactoglobulin assembles into amyloid through sequential aggregated intermediates.

We have investigated the aggregation and amyloid fibril formation of bovine beta-lactoglobulin variant A, with a focus on the early stages of aggregation. We used noncovalent labeling with thioflavin T and 1-anilino-8-naphthalenesulfonate to follow the conformational changes occurring in beta-lactoglobulin during aggregation using time resolved luminescence. 1-Anilino-8-naphthalenesulfonate monitored the involvement of the hydrophobic core/calyx of beta-lactoglobulin in the aggregation process.