The extensive application of profenofos (PFF), a widely used organophosphorus pesticide (OP), has raised significant environmental and health concerns due to its accumulation in ecosystems and its inhibitory effects on acetylcholinesterase in humans. Despite advancements in analytical technologies, currently available chromatography and electrochemical assays often involve complex procedures, high costs, and specialized equipment, limiting their applicability for routine and on-site PFF monitoring. Here, we report a novel self-cascade nanozyme-based colorimetric biosensor employing a hierarchically macroporous Ce-MOF (HMUiO-66(Ce)) with integrated phosphoester hydrolase (PEH)- and oxidase (OXD)-like activities.
View Article and Find Full Text PDFACS Appl Mater Interfaces
April 2025
In situ encapsulation of enzymes within a metal-organic framework (MOF) represents a promising technique for engineering robust biocatalysts. However, the success of enzyme encapsulation is often constrained by intricate interfacial interactions between enzyme surfaces and MOF precursors, limiting the versatility of this MOF method. Herein, we introduce a phase transition strategy for encapsulating enzymes within a Zn-HHTP framework, demonstrating its effectiveness across a wide range of enzymes irrespective of their surface chemistry.
View Article and Find Full Text PDFSpatial immobilization of fragile enzymes using a nanocarrier is an efficient means to design heterogeneous biocatalysts, presenting superior stability and recyclability to pristine enzymes. An immobilized enzyme, however, usually compromises its catalytic activity because of inevasible mass transfer issues and the unfavorable conformation changes in a confined environment. Here, we describe a synergetic metal-organic framework pore-engineering strategy to trap lipase (an important hydrolase), which confers lipase-boosted stability and activity simultaneously.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
February 2024
Utilizing covalent organic framework (COF) as a hypotoxic and porous scaffold to encapsulate enzyme (enzyme@COF) has inspired numerous interests at the intersection of chemistry, materials, and biological science. In this study, we report a convenient scheme for one-step, aqueous-phase synthesis of highly crystalline enzyme@COF biocatalysts. This facile approach relies on an ionic liquid (2 μL of imidazolium ionic liquid)-mediated dynamic polymerization mechanism, which can facilitate the in situ assembly of enzyme@COF under mild conditions.
View Article and Find Full Text PDFEnzyme immobilization into porous frameworks is an emerging strategy for enhancing the stability of dynamic conformation and prolonging the lifespan of enzymes. Here, we present a protocol for a de novo mechanochemistry-guided assembly strategy for enzyme encapsulation using covalent organic frameworks. We describe steps for mechanochemical synthesis, enzyme loading measurements, and material characterizations.
View Article and Find Full Text PDFEnzymes are outstanding natural catalysts with exquisite 3D structures, initiating countless life-sustaining biotransformations in living systems. The flexible structure of an enzyme, however, is highly susceptible to non-physiological environments, which greatly limits its large-scale industrial applications. Seeking suitable supports to immobilize fragile enzymes is one of the most efficient routes to ameliorate the stability problem.
View Article and Find Full Text PDFThe chemokine family plays an important role in the growth, invasion, and metastasis of tumors. However, most studies have only focused on a few genes or a few gene loci, and thus could not reveal the associations between functional polymorphisms of chemokine family members and tumor progression. This study aimed to determine the associations between single nucleotide polymorphisms (SNPs) of chemokine family members and the prognosis of esophageal cancer (EC).
View Article and Find Full Text PDFOncol Lett
April 2019
Gastric cancer (GC) is the third leading cause of cancer-associated mortality. In a previous study, we identified that α-enolase (ENO1) promoted cell migration in GC, but the underlying molecular mechanisms remain to be fully elucidated. In the present study, small interfering RNAs were identified to interfere with ENO1 expression.
View Article and Find Full Text PDFOur preview studies showed TPI gene which encodes the Triosephosphate isomerase was overexpressed in human gastric cancer (GC) tissues. However, the potential molecular mechanisms how TPI influences the GC development is not clear. Here, we performed global gene expression profiling for TPI knockdown using microarrays in human GC cell line MGC-803 cells.
View Article and Find Full Text PDFOncol Rep
September 2017
Triosephosphate isomerase (TPI) is highly expressed in many types of human tumors and is involved in migration and invasion of cancer cells. However, TPI clinicopathological significance and malignant function in gastric cancer (GC) have not been well defined. The present study aimed to examine TPI expression in GC tissue and its biological functions.
View Article and Find Full Text PDFMedicine (Baltimore)
May 2017
Triosephosphate isomerase (TPI) is highly expressed in many human cancers and is involved in migration and invasion of cancer cells. However, TPI clinicopathological significance and prognostic value in gastric cancer (GC) are not yet well defined. The aim of the present work was to evaluate TPI expression in GC tissue and its prognostic value in GC patients.
View Article and Find Full Text PDFTwo unsymmetrical oxovanadium complexes incorporating salicylaldehyde derivate and phenanthroline [VO(DESAA)(phen)] (1), (DESAA = 4-(diethylamino)salicylaldehyde anthranilic acid, phen = phenanthroline) and [VO(CLSAA)(phen)] (2), (CLSAA = 5-chlorosalicylaldehyde anthranilic acid)] have been synthesized and characterized. The interactions of the complexes with CT-DNA were studied using different techniques. Complexes 1 and 2 interact with CT-DNA by intercalative modes and can efficiently cleave pBR322 DNA after light irradiation.
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