Pathogens pose a serious threat to public and population health, leading to serious outbreak and spread of diseases irrespective of the region. The capability to directly, sensitively, and specifically detect viable pathogens in low numbers in food and clinical samples is very desirable but remains a challenge. In this work, we present a novel assay of a combination of an aptamer-based allosteric probe and hairpin switch-controlled T7 RNA polymerase-based isothermal transcription amplification, which enables rapid, ultrasensitive, label-free detection of direct pathogens. It can detect as low as 73.2 CFU/mL. Moreover, with the usage of the proposed assay, sensitive quantification of in milk samples has been achieved, showing significant potential as a simple and sensitive tool to quantify pathogens in milk and other foods.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.analchem.4c02413 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Lycorine esters exert anti-HCoV-OC43 effect through reversibly acylating cysteine residue in the nsp 12 NiRAN domain.
Bioorg Chem
December 2024
State Key Laboratory of Bioactive Substances and Functions of Natural Medicines, Institute of Medicinal Biotechnology, Peking Union Medical College and Chinese Academy of Medical Sciences, Beijing 100050, China. Electronic address:
By introducing ester warheads into the hydroxyl groups in lycorine (1), three types of lycorine mono-ester or di-ester analogues were synthesized and evaluated for their antiviral activities against HCoV-OC43. Most of them showed higher selective indexes (SI) than 1, up to nearly 14 times. Using compound 6b as a probe, we firstly demonstrated that lycorine esters directly targeted nidovirus RdRp-associated nucleotidyltransferase (NiRAN) domain in the non-structural protein 12 (nsp 12) by reversibly acylating Cys12 to induce the shrink of NiRAN pocket and block the viral replication, different from the known RdRp inhibitors.
View Article and Find Full Text PDFDesign of allosteric modulators that change GPCR G protein subtype selectivity.
Res Sq
December 2024
Department of Pharmacology, University of Minnesota Twin Cities, Minneapolis, MN, USA.
G protein-coupled receptors (GPCRs), the largest family of drug targets, can signal through 16 subtypes of Gα proteins. Biased compounds that selectively activate therapy-relevant pathways promise to be safer, more effective medications. The determinants of bias are poorly understood, however, and rationally-designed, G protein-subtype-selective compounds are lacking.
View Article and Find Full Text PDFAlphaFold2-Based Characterization of Apo and Holo Protein Structures and Conformational Ensembles Using Randomized Alanine Sequence Scanning Adaptation: Capturing Shared Signature Dynamics and Ligand-Induced Conformational Changes.
Int J Mol Sci
December 2024
Keck Center for Science and Engineering, Schmid College of Science and Technology, Chapman University, Orange, CA 92866, USA.
Proteins often exist in multiple conformational states, influenced by the binding of ligands or substrates. The study of these states, particularly the apo (unbound) and holo (ligand-bound) forms, is crucial for understanding protein function, dynamics, and interactions. In the current study, we use AlphaFold2, which combines randomized alanine sequence masking with shallow multiple sequence alignment subsampling to expand the conformational diversity of the predicted structural ensembles and capture conformational changes between apo and holo protein forms.
View Article and Find Full Text PDFA goldilocks computational protocol for inhibitor discovery targeting DNA damage responses including replication-repair functions.
Front Mol Biosci
November 2024
Department of Molecular and Cellular Oncology, University of Texas MD Anderson Cancer Center, Houston, TX, United States.
While many researchers can design knockdown and knockout methodologies to remove a gene product, this is mainly untrue for new chemical inhibitor designs that empower multifunctional DNA Damage Response (DDR) networks. Here, we present a robust Goldilocks (GL) computational discovery protocol to efficiently innovate inhibitor tools and preclinical drug candidates for cellular and structural biologists without requiring extensive virtual screen (VS) and chemical synthesis expertise. By computationally targeting DDR replication and repair proteins, we exemplify the identification of DDR target sites and compounds to probe cancer biology.
View Article and Find Full Text PDFDistinct modulation of calcium-activated chloride channel TMEM16A by drug-binding sites.
Proc Natl Acad Sci U S A
December 2024
Channelopathy Research Center, Dongguk University College of Medicine, Goyang 10326, Republic of Korea.
Article Synopsis
- * Using magnolol and honokiol, researchers identified two distinct drug-binding sites on TMEM16A—one in the pore region and another nonpore pocket, each interacting differently with the channel.
- * The study highlights that out of 17 inhibitors tested, a majority acted as pore blockers, revealing the significance of the nonpore pocket and informing future drug development strategies.
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!