Aptamer 学术简报 — infectious_disease — 2026-08-27

自动生成 by RBTX Aptamer Tracker v0.1。 子主题 infectious_disease:近 14 天 11 篇命中(aptamer 池 201 篇)。

评分公式:composite = 0.45×log(IF) + 0.35×log(cites_velocity) + 0.10×social + 0.10×recency_bonus;满分 100。


#1 [11.5] High-ThroughputOn-Chip Screening Enables Rapid Adaptationof DNA Aptamers to SARS-CoV-2 Evolution

Abstract Rapid pathogen evolution threatens public health by eroding the effectiveness of vaccines, therapeutics, and diagnostic tools. Although spike-protein-targeting monoclonal antibodies (mAbs) were developed within 10–12 months of the initial outbreak to serve as key theranostic agents, their redesign has struggled to keep pace with viral e...


#2 [11.5] Chimeric ascorbic acid phosphate-releasing nucleotide probes for isothermal signal-amplified protein detection.

Protein detection is essential for disease diagnosis and biomarker analysis but often relies on antibodies and sophisticated instrumentation. Here, we report a signal-amplified protein detection strategy based on chimeric ascorbic acid-2-phosphate (AAP)-releasing nucleotide probes and strand displacement amplification (SDA). Two tetraphosphate n...


#3 [10.8] Surface-confined CRISPR-Cas12a biosensor with metal-enhanced fluorescence for rapid and ultrasensitive detection of SARS-CoV-2 nucleocapsid protein.

CRISPR-Cas12a integrated with nanomaterials has formulated powerful biosensors for viral protein detection, addressing the urgent need for point-of-care diagnostics. However, existing platforms are hindered by either multi-step separation procedures or insufficient signal amplification, limiting their sensitivity and practicality. Here, we repor...


#4 [10.1] Single-Particle Tracking and Positional Phenotyping Reveal Variant-Specific Early Checkpoints in SARS-CoV-2 Cell Entry.

Bulk assays of SARS-CoV-2 entry obscure individual virions and conflate binding with internalization. We developed a quantitative single-particle imaging assay that classifies fluorescent virus-like particles (VLPs) as surface, crossing, or internal on HEK293T-ACE2 cells, separating binding from internalization. Comparing G614 and Omicron BA.5 S...


#5 [8.8] Ag85A-PEGylated Propolis Nanoparticles Exhibit Intracellular Antimycobacterial and Host-Protective Activities Against Mycobacterium tuberculosis.

Tuberculosis (TB), caused by the intracellular pathogen Mycobacterium tuberculosis (Mtb), remains a major global health challenge. The prolonged duration of treatment and the emergence of multidrug-resistant strains have highlighted the need for alternative therapeutic strategies. This study investigated the therapeutic potential of Ag85A aptame...


#6 [7.3] High-Sensitivity Magnetic Particle Spectroscopy Platform for Precise, Specific, and Rapid Detection of Infectious Disease and Cancer-Related Biomarkers.

Accurate biosensing using magnetic particle spectroscopy (MPS) depends on the interplay between biomolecular binding and the fidelity of the measurement system. MPS enables wash-free, label-free biosensing by monitoring Brownian relaxation-induced changes in magnetic nanoparticle (MNP) dynamics. However, its practical performance is often limite...


#7 [6.7] A label-free and highly sensitive fluorescence aptasensor for enrofloxacin detection based on G-triplex-mediated signal amplification.

Enrofloxacin (ENR), a third-generation fluoroquinolone veterinary antibiotic, is widely used in aquaculture and animal husbandry for bacterial infection control due to its broad-spectrum antimicrobial activity, potent bactericidal efficacy, and cost-effectiveness. However, its excessive and non-standard use has caused widespread residues in anim...


#8 [5.3] Threomer Inhibition of S1−ACE2 Binding

Abstract The interaction between the receptor binding domain (RBD) of the SARS-CoV-2 spike protein (S1) and human ACE2 receptor is essential for viral entry into host epithelial cells and a key target for drug discovery. Here, we describe the evolution of a threomer, a base-modified version of threose nucleic acid (TNA), that binds to the S1 pro...



Methodology