Dong S

References (22)

Title : Design, synthesis, and biological evaluation of novel tryptanthrin derivatives as selective acetylcholinesterase inhibitors for the treatment of Alzheimer's disease - Xia_2023_Bioorg.Chem_143_106980
Author(s) : Xia J , Dong S , Yang L , Wang F , Xing S , Du J , Li Z
Ref : Bioorg Chem , 143 :106980 , 2023
Abstract : Two novel series of tryptanthrin (TRYP) derivatives were designed and synthesized as multifunctional agents for the treatment of Alzheimer's disease (AD). Inhibition assay against cholinesterase (ChE) indicated that these derivatives can act as acetylcholinesterase (AChE) inhibitors with selectivity over butyrylcholinesterase (BuChE). Among them, n1 exhibited the most excellent ChE inhibitory potency (AChE, IC(50) = 12.17 +/- 1.50 nM; BuChE, IC(50) = 6.29 +/- 0.48 micro; selectivity index = 517). Molecular docking studies indicated that compound n1 can interact with amino acid residues in the catalytic active site and peripheral anionic site of AChE and the molecular dynamics (MD) simulation studies demonstrated that the AChE-n1 complex had good stability. N1 also exhibited anti-amyloid-beta (Abeta) aggregation (63.48 % +/- 1.02 %, 100 micro) and anti-neuroinflammation activity (NO, IL-1beta, TNF-alpha; IC(50) = 2.13 +/- 0.54 micro, 2.21 +/- 0.37 micro, 2.47 +/- 0.07 micro, respectively), and n1 had neuroprotective and metal-chelating properties. Further studies indicated n1 had proper blood-brain barrier permeability in the Parallel artificial membrane permeation assay. In vivo studies found that n1 effectively improved learning and memory impairment in scopolamine-induced AD mouse models. Nissl staining ofmice hippocampaltissue sections revealed that n1 restored neuronal cells in the hippocampus CA3 and CA1 regions. These findings suggested that n1 can be a promising compound for further development of multifunctional agents for AD treatment.
ESTHER : Xia_2023_Bioorg.Chem_143_106980
PubMedSearch : Xia_2023_Bioorg.Chem_143_106980
PubMedID: 38006789

Title : Discovery of Novel Tryptanthrin Derivatives with Benzenesulfonamide Substituents as Multi-Target-Directed Ligands for the Treatment of Alzheimer's Disease - Wang_2023_Pharmaceuticals.(Basel)_16_
Author(s) : Wang G , Du J , Ma J , Liu P , Xing S , Xia J , Dong S , Li Z
Ref : Pharmaceuticals (Basel) , 16 : , 2023
Abstract : Based on the multi-target-directed ligands (MTDLs) approach, two series of tryptanthrin derivatives with benzenesulfonamide substituents were evaluated as multifunctional agents for the treatment of Alzheimer's disease (AD). In vitro biological assays indicated most of the derivatives had good cholinesterase inhibitory activity and neuroprotective properties. Among them, the target compound 4h was considered as a mixed reversible dual inhibitor of acetylcholinesterase (AChE, IC(50) = 0.13 +/- 0.04 microM) and butyrylcholinesterase (BuChE, IC(50) = 6.11 +/- 0.15 microM). And it could also potentially prevent the generation of amyloid plaques by inhibiting self-induced Abeta aggregation (63.16 +/- 2.33%). Molecular docking studies were used to explore the interactions of AChE, BuChE, and Abeta. Furthermore, possessing significant anti-neuroinflammatory potency (NO, IL-1beta, TNF-alpha; IC(50) = 0.62 +/- 0.07 microM, 1.78 +/- 0.21 microM, 1.31 +/- 0.28 microM, respectively) reduced ROS production, and chelated biometals were also found in compound 4h. Further studies showed that 4h had proper blood-brain barrier (BBB) permeability and suitable in vitro metabolic stability. In in vivo study, 4h effectively ameliorated the learning and memory impairment of the scopolamine-induced AD mice model. These findings suggested that 4h may be a promising compound for further development as a multifunctional agent for the treatment of AD.
ESTHER : Wang_2023_Pharmaceuticals.(Basel)_16_
PubMedSearch : Wang_2023_Pharmaceuticals.(Basel)_16_
PubMedID: 37895939

Title : Recent Progress in the Mechanism and Engineering of alpha\/beta Hydrolases for Chiral Chemical Production - Qiu_2023_Catalysts_13_288
Author(s) : Qiu M , Dong S , Cui Q , Feng Y , Xuan J
Ref : Catalysts , 13 :288 , 2023
Abstract : Chiral compounds are valuable industrial products and intermediates, and the production of chemicals with high enantiopurity is one of the major objects in asymmetric catalysis. Compared with traditional chemical synthesis, enzymatic synthesis can produce chiral molecules under sustainable conditions which are much greener, more economical, and more environmentally friendly. The superfamily of alpha/beta hydrolases includes a lot of diverse enzymes showing excellent chemo-, regio-, and enantio-selectivity in asymmetric synthesis and many of them are biocatalysts in industry. This review outlines the current knowledge of the structures and reaction mechanism of alpha/beta hydrolases and summarizes the screening and protein engineering efforts to develop biocatalysts for chiral chemicals production in recent years. Other strategies such as whole-cell catalysis and protein immobilization to improve the performance of alpha/beta hydrolases are also discussed. The progress in biocatalyst development based on alpha/beta hydrolases will promote the biosynthesis of chiral compounds, thus contributing to the green and sustainable development of the chemical and pharmaceutical industry.
ESTHER : Qiu_2023_Catalysts_13_288
PubMedSearch : Qiu_2023_Catalysts_13_288
PubMedID:

Title : Discovery of novel deoxyvasicinone derivatives with benzenesulfonamide substituents as multifunctional agents against Alzheimer's disease - Dong_2023_Eur.J.Med.Chem_264_116013
Author(s) : Dong S , Xia J , Wang F , Yang L , Xing S , Du J , Zhang T , Li Z
Ref : Eur Journal of Medicinal Chemistry , 264 :116013 , 2023
Abstract : A series of deoxyvasicinone derivatives with benzenesulfonamide substituents were designed and synthesized to find a multifunctional anti-Alzheimer's disease (AD) drug. The results of the biological activity evaluation indicated that most compounds demonstrated selective inhibition of acetylcholinesterase (AChE). Among them, g17 exhibited the most potent inhibitory effect on AChE (IC(50) = 0.24 +/- 0.04 microM). Additionally, g17 exhibited promising properties as a metal chelator and inhibitor of amyloid beta peptides self-aggregation (68.34 % +/- 1.16 %). Research on oxidative stress has shown that g17 displays neuroprotective effects and effectively suppresses the intracellular accumulation of reactive oxygen species. Besides, g17 demonstrated remarkable anti-neuroinflammatory effects by significantly reducing the production of pro-inflammatory cytokines (such as NO, IL-1beta, and TNF-alpha) and inhibiting the expression of inflammatory mediators iNOS and COX-2. In vivo studies showed that g17 significantly improved AD model mice's cognitive and memory abilities. Histological examination of mouse hippocampal tissue sections using hematoxylin and eosin staining revealed that g17 effectively mitigates neuronal damage. Considering the multifunctional properties of g17, it is regarded as a promising lead compound for treating AD.
ESTHER : Dong_2023_Eur.J.Med.Chem_264_116013
PubMedSearch : Dong_2023_Eur.J.Med.Chem_264_116013
PubMedID: 38052155

Title : A Novel Nomogram for Predicting Risk Factors and Outcomes in Bloodstream Infections Caused by Klebsiella pneumoniae - Chen_2022_Infect.Drug.Resist_15_1317
Author(s) : Chen Y , Ying S , Jiang L , Dong S , Dai J , Jin X , Yu W , Qiu Y
Ref : Infect Drug Resist , 15 :1317 , 2022
Abstract : BACKGROUND: Our study aimed to explore the risk factors in bloodstream infections Klebsiella pneumoniae (BSI-KP) patients and establish nomograms to predict the probability of BSI-CRKP and the prognosis of BSI-KP. METHODS: A total of 252 BSI-KP patients were enrolled from a tertiary teaching hospital between January 1, 2015, and May 31, 2020. Risk factors associated with BSI-CRKP and factors associated with the 30-day mortality were identified using LASSO analysis, univariate and multivariate analysis. RESULTS: There were 121 (48.0%) patients with carbapenem-resistant K. pneumoniae (CRKP) and 131 (52.0%) patients with carbapenem-susceptible K. pneumoniae (CSKP). The multivariate logistic regression analysis demonstrated that gastric tube indwelling before BSI (OR=2.442, P=0.043) and more types of antibiotics use before BSI (OR=1.305, P=0.009) were independent risk factors for BSI-CRKP. And previous transplantations, prior ICU stay, gastric tube indwelling before BSI, more types of antibiotics use before BSI, lower Hb and cholinesterase were associated with CRKP-BSI. The C-index of models indicated its good accuracy (C-index 0.816, 95% CI 0.763-0.868). In patients with BSI-CRKP, further logistic regression analysis revealed urinary catheterization (OR=0.298, P=0.017) was found to be an independent risk factor for 30-day mortality, while ceftazidime/avibactam use (OR=8.438, P=0.003) was an independent favorable prognostic factor. The nomogram predicated CRKP, ICU hospitalization, more types of antibiotics use, tigecycline, PLT, urinary catheterization were associated with 30-day mortality in patients with BSI-KP. The discriminative ability of the predictive model, as assessed by C-index, was 0.813 (95% CI: 0.780-0.867). CONCLUSION: Previous transplantations, prior ICU stay, gastric tube indwelling before BSI, more types of antibiotics use before BSI, lower Hb and cholinesterase represent significant risk factors for the development of BSI-CRKP. Our nomogram predicated thrombocytopenia was a sign for poor prognosis. Tigecycline resulted in higher mortality for patients with BSI-KP. Rational use of nomograms may help clinicians make better Clinical decisions when treating BSI-KP patients.
ESTHER : Chen_2022_Infect.Drug.Resist_15_1317
PubMedSearch : Chen_2022_Infect.Drug.Resist_15_1317
PubMedID: 35378894

Title : Mutation in BrGGL7 gene encoding a GDSL esterase \/ lipase causes male sterility in Chinese cabbage (Brassica rapa L. ssp. pekinensis) - Zhao_2022_Theor.Appl.Genet_135_3323
Author(s) : Zhao Y , Huang S , Zou J , Dong S , Wang N , Feng H
Ref : Theor Appl Genet , _135 :3323 , 2022
Abstract : MutMap and KASP analyses revealed that the BrGGL7 gene is responsible for the male-sterile trait of ftms1 in Chinese cabbage, with functional verification in Arabidopsis. The application of a male-sterile line is an ideal approach of hybrid seed production in Chinese cabbage. In this study, we obtained a male-sterile mutant (ftms1) from the double haploid line 'FT' using ethyl methane sulfonate (EMS) mutagenesis. The mutant was completely sterile due to abnormal enlargement and vacuolization of the tapetum cells. A single recessive nuclear gene was found to control male sterility in the mutant, while MutMap and KASP analyses identified BraA05g022470.3C (BrGGL7), which encodes a GDSL esterase / lipase, as the candidate mutant gene. A single nucleotide substitution from C to T occurred within the domain of BrGGL7 in ftms1, resulting in premature translation termination in the fourth exon. Meanwhile, qRT-PCR analysis indicated that BrGGL7 was prominently expressed in the anothers, and expression was greater in the wild-type 'FT' than ftms1. Genetic complementation of the orthologous Arabidopsis ggl7 mutant further confirmed the role of BrGGL7 in pollen development. These findings suggest that BrGGL7 plays a fundamental role in pollen formation, providing important insight into the molecular mechanisms underlying male sterility in Chinese cabbage.
ESTHER : Zhao_2022_Theor.Appl.Genet_135_3323
PubMedSearch : Zhao_2022_Theor.Appl.Genet_135_3323
PubMedID: 35840736

Title : A novel pomegranate-inspired bifunctional electrode materials design for acetylcholinesterase biosensor and methanol oxidation reaction - Wei_2022_Bioelectrochemistry_145_108094
Author(s) : Wei W , Tang H , Dong S , Fu Y , Huang T
Ref : Bioelectrochemistry , 145 :108094 , 2022
Abstract : A pomegranate-inspired bifunctional electrode material based on Ni/NiO nanoparticle embedded in nitrogen-doped, partially graphitized carbon framework (Ni/NiO@NPGC) was designed and prepared for the construction of novel electrochemical biosensor and methanol oxidation reaction (MOR). Profiting from itsspecialstructureandfunction, Ni/NiO@NPGC was employed as a matrix immobilizing acetylcholinesterase (AChE) for methyl parathion (MP) sensor. The developed biosensor was proved to have wide linear range (1.0 x 10(-14)-1.0 x 10(-8) g mL(-1)), low detection limit (3.5 x 10(-15) g mL(-1)), and good stability for the determination of MP in practical samples. In addition, the Ni/NiO@NPGC electrode exhibited high electrocatalytic activity (specific activity 73.1 mA cm(-2)) and durability for the MOR in alkaline medium. The results were mainly attributed to the pomegranate-like architecture structure with pyridinic N and carbon frame of Ni/NiO@NPGC, which ensured the electrochemical activities of all nanoparticles and immobilization of enzyme. In addition, the metal oxide was well dispersed to prevent from self-agglomeration and kept mass transfer paths. The work provides a reference for the development of high-performance bifunctional electrode material for the biosensor and MOR.
ESTHER : Wei_2022_Bioelectrochemistry_145_108094
PubMedSearch : Wei_2022_Bioelectrochemistry_145_108094
PubMedID: 35299151

Title : A Simple Aptamer SERS Sensor Based on Mesoporous Silica for the Detection of Chlorpyrifos - Dong_2022_Foods_11_
Author(s) : Dong S , Shi Q , He K , Wu J , Zhu Z , Feng J
Ref : Foods , 11 : , 2022
Abstract : Chlorpyrifos is an organophosphorus insecticide, which can be used to control a variety of chewing and piercing mouthparts pests in agricultural production. It can destroy the normal nerve impulse conduction by inhibiting the activity of acetylcholinesterase or cholinesterase in the nerves, causing a series of poisoning symptoms. In order to achieve the quantitative analysis of chlorpyrifos residues in agricultural products, an aptamer-controlled signal molecule release method was developed in this study. The signal molecule 4-ATP of surface-enhanced Raman spectroscopy (SERS) was loaded into aminated mesoporous silica nanoparticles (MSNs-NH(2)) prepared by the one pot method, and then coated with an aptamer of chlorpyrifos through electrostatic interaction. The specific binding of the aptamer and chlorpyrifos led to the release of 4-ATP, and the amount of 4-ATP released was positively correlated with the amount of chlorpyrifos. Finally, the standard curve of chlorpyrifos quantitative detection based on SERS was established. Meanwhile, Ag-carrying mesoporous silica (Ag@MSNs) was prepared as the reinforcement substrate for SERS detection. The results showed that there was a good linear correlation between the Raman intensity and the concentration of chlorpyrifos at 25-250 ng/mL, and the limit of detection (LOD) was 19.87 ng/mL. The recoveries of chlorpyrifos in the apple and tomato samples were 90.08-102.2%, with RSD < 3.32%. This method has high sensitivity, specificity, reproducibility and stability, and can be used for the quantitative detection of chlorpyrifos in the environment and agricultural products.
ESTHER : Dong_2022_Foods_11_
PubMedSearch : Dong_2022_Foods_11_
PubMedID: 36359944

Title : Functional Characterization and Crystal Structure of the Bifunctional Thioesterase Catalyzing Epimerization and Cyclization in Skyllamycin Biosynthesis - Yu_2021_ACS.Catalysis_11_11733
Author(s) : Yu J , Juan S , Chi C , Liu T , Geng T , Cai Z , Dong W , Shi C , Ma X , Zhang Z , Xing B , Jin H , Zhang L , Dong S , Yang D , Ma M
Ref : ACS Catal , 11 :11733 , 2021
Abstract : The d-amino acid residues are hallmark building blocks of nonribosomal peptides. Here, we report the bifunctional thioesterase domain (TE domain) Skyxy-TE that catalyzes both epimerization and cyclization in skyllamycin biosynthesis. Skyxy-TE specifically catalyzes the epimerization of the C-terminal l-amino acid residue of the linear substrate, then catalyzes regioselective intramolecular cyclization. The crystal structure of Skyxy-TE was solved at 2.25 and site-directed mutagenesis was performed, revealing key residues involved in the epimerization and cyclization. This study expands the understanding of the versatile TE domains and facilitates chemoenzymatic synthesis or combinatorial biosynthesis in the future.
ESTHER : Yu_2021_ACS.Catalysis_11_11733
PubMedSearch : Yu_2021_ACS.Catalysis_11_11733
PubMedID:
Gene_locus related to this paper: strsq-a0a1j0r317

Title : Computational redesign of a PETase for plastic biodegradation under ambient condition by the GRAPE strategy - Cui_2021_ACS.Catal_11_1340
Author(s) : Cui Y , Chen Y , Liu X , Dong S , Tian Y , Qiao Y , Mitra R , Han J , Li C , Han X
Ref : ACS Catal , 11 :1340 , 2021
Abstract : Nature has provided a fantastic array of enzymes that are responsible for essential biochemical functions but not usually suitable for technological applications. Not content with the natural repertoire, protein engineering holds promise to extend the applications of improved enzymes with tailored properties. However, engineering of robust proteins remains a difficult task since the positive mutation library may not cooperate to reach the target function in most cases owing to the ubiquity of epistatic effects. The main demand lies in identifying an efficient path of accumulated mutations. Herein, we devised a computational strategy (greedy accumulated strategy for protein engineering, GRAPE) to improve the robustness of a PETase from Ideonella sakaiensis. A systematic clustering analysis combined with greedy accumulation of beneficial mutations in a computationally derived library enabled the redesign of a variant, DuraPETase, which exhibits an apparent melting temperature that is drastically elevated by 31 C and a strikingly enhanced degradation toward semicrystalline poly(ethylene terephthalate) (PET) films (30%) at mild temperatures (over 300-fold). Complete biodegradation of 2 g/L microplastics to water-soluble products under mild conditions is also achieved, opening up opportunities to steer the biological degradation of uncollectable PET waste and further conversion of the resulting monomers to high-value molecules. The crystal structure revealed the individual mutation match with the design model. Concurrently, synergistic effects are captured, while epistatic interactions are alleviated during the accumulation process. We anticipate that our design strategy will provide a broadly applicable strategy for global optimization of enzyme performance.
ESTHER : Cui_2021_ACS.Catal_11_1340
PubMedSearch : Cui_2021_ACS.Catal_11_1340
PubMedID:
Gene_locus related to this paper: idesa-peth

Title : Synthesis and Structure-Activity Relationships of 3-Arylisoquinolone Analogues as Highly Specific hCES2A Inhibitors - Zhao_2021_ChemMedChem_16_388
Author(s) : Zhao Y , Xiong Y , Dong S , Guan X , Song Y , Yang Y , Zou K , Li Z , Zhang Y , Fang S , Li B , Zhu W , Chen K , Jia Q , Ge G
Ref : ChemMedChem , 16 :388 , 2021
Abstract : Mammalian carboxylesterases (CES) are key enzymes that participate in the hydrolytic metabolism of various endogenous and exogenous substrates. Human carboxylesterase 2A (hCES2A), mainly distributed in the small intestine and colon, plays a significant role in the hydrolysis of many drugs. In this study, 3-arylisoquinolones 3h [3-(4-(benzyloxy)-3-methoxyphenyl)-7,8-dimethoxyisoquinolin-1(2H)-one] and 4a [3-(4-(benzyloxy)-3-methoxyphenyl)-4-bromo-7,8-dimethoxyisoquinolin-1(2H)-one] were found to have potent inhibitory effects on hCES2A (IC(50) =0.68microM, K(i) =0.36microM) and excellent specificity (more than 147.05-fold over hCES1A). Moreover, 4a exhibited threefold improved inhibition on intracellular hCES2A in living HepG2 cells relative to 3h, with an IC(50) value of 0.41microM. Results of inhibition kinetics studies and molecular docking simulations demonstrate that both 3h and 4a can bind to multiple sites on hCES2A, functioning as mixed inhibitors. Structure-activity relationship analysis revealed that the lactam moiety on the B ring is crucial for specificity towards hCES2A, while a benzyloxy group is optimal for hCES2A inhibitory potency; the introduction of a bromine atom may enhance cell permeability, thereby increasing the intracellular hCES2A inhibitory activity.
ESTHER : Zhao_2021_ChemMedChem_16_388
PubMedSearch : Zhao_2021_ChemMedChem_16_388
PubMedID: 32935462

Title : Organophosphate Diesters (Di-OPEs) Play a Critical Role in Understanding Global Organophosphate Esters (OPEs) in Fishmeal - Li_2020_Environ.Sci.Technol_54_12130
Author(s) : Li X , Zhao N , Fu J , Liu Y , Zhang W , Dong S , Wang P , Su X
Ref : Environ Sci Technol , 54 :12130 , 2020
Abstract : Organophosphate triesters (tri-OPEs) have recently been widely identified in aquatic ecosystems, but information on their organophosphate diester (di-OPE) metabolites is sparsely available. Herein, uniform fishmeal products were collected across the globe (the U.S., China, Europe, South America, and Southeast Asia). Sixteen representative tri-OPEs and eight di-OPEs were investigated to reveal whether industrial production, metabolism, environmental persistence, or physicochemical properties are the key factors influencing their environmental burden and distribution. Tri-OPEs and di-OPEs were 100% detected in fishmeal, with bis(2-chloroethyl) hydrogen phosphate (BCEP) and bis(1,3-dichloro-2-propyl) phosphate (BDCIPP) at discernible levels in marine fauna for the first time. Average concentration of di-OPEs (49.6 +/- 27.5 ng/g dw) was of the same order of magnitude as that of tri-OPEs (59.3 +/- 92.2 ng/g dw). Geographical-specific distributions of tris(2-chloroethyl) phosphate (TCEP), tris(2-chloroisopropyl) phosphate (TCIPP), triphenyl phosphate (TPhP), tris(2-butoxyethyl) phosphate (TBOEP), and 2-ethylhexyl diphenyl phosphate (EHDPP) were statistically significant (p < 0.05). Mean concentration ratios ranged from 0.087 for the BCEP-TCEP pair to 507 for the dimethyl phosphate (DMP)-trimethyl phosphate (TMP) pair. Only the TPhP-diphenyl phosphate (DPhP) pair presented a strong positive linear correlation (r = 0.731; p < 0.01), and DPhP was proved a degradation origin. Commercial sources had a significant overall impact on distribution patterns of the DMP-TMP and the dibutyl phosphate (DnBP) - tri-n-butyl phosphate (TnBP) pairs, whereas biotic transformation and abiotic stability profoundly influenced the bis(2-ethylhexyl) phosphate (BEHP)-tris(2-ethylhexyl) phosphate (TEHP), the bis(1-chloro-2-propyl) phosphate (BCIPP)-TCIPP, and the BCEP-TCEP pairs. Di-OPEs are critical to understand environmental behavior of tri-OPEs in marine fauna.
ESTHER : Li_2020_Environ.Sci.Technol_54_12130
PubMedSearch : Li_2020_Environ.Sci.Technol_54_12130
PubMedID: 32936633

Title : Potential of esterase DmtH in transforming plastic additive dimethyl terephthalate to less toxic mono-methyl terephthalate - Cheng_2020_Ecotoxicol.Environ.Saf_187_109848
Author(s) : Cheng X , Dong S , Chen D , Rui Q , Guo J , Dayong W , Jiang J
Ref : Ecotoxicology & Environmental Safety , 187 :109848 , 2020
Abstract : Dimethyl terephthalate (DMT) is a primary ingredient widely used in the manufacture of polyesters and industrial plastics; its environmental fate is of concern due to its global use. Microorganisms play key roles in the dissipation of DMT from the environment; however, the enzymes responsible for the initial transformation of DMT and the possible altered toxicity due to this biotransformation have not been extensively studied. To reduce DMT toxicity, we identified the esterase gene dmtH involved in the initial transformation of DMT from the AOPP herbicide-transforming strain Sphingobium sp. C3. DmtH shows 24-41% identity with alpha/beta-hydrolases and belongs to subfamily V of bacterial esterases. The purified recombinant DmtH was capable of transforming DMT to mono-methyl terephthalate (MMT) and potentially transforming other p-phthalic acid esters, including diallyl terephthalate (DAT) and diethyl terephthalate (DET). Using C. elegans as an assay model, we observed the severe toxicity of DMT in inducing reactive oxygen species (ROS) production, decreasing locomotion behavior, reducing lifespan, altering molecular basis for oxidative stress, and inducing mitochondrial stress. In contrast, exposure to MMT did not cause obvious toxicity, induce oxidative stress, and activate mitochondrial stress in nematodes. Our study highlights the usefulness of Sphingobium sp. C3 and its esterase DmtH in transforming p-phthalic acid esters and reducing the toxicity of DMT to organisms.
ESTHER : Cheng_2020_Ecotoxicol.Environ.Saf_187_109848
PubMedSearch : Cheng_2020_Ecotoxicol.Environ.Saf_187_109848
PubMedID: 31670182
Gene_locus related to this paper: 9sphn-a0a3s8nd90

Title : Sublethal effects of imidacloprid on the performance of the bird cherry-oat aphid Rhopalosiphum padi - Li_2018_PLoS.One_13_e0204097
Author(s) : Li W , Lu Z , Li L , Yu Y , Dong S , Men X , Ye B
Ref : PLoS ONE , 13 :e0204097 , 2018
Abstract : The bird cherry-oat aphid, Rhopalosiphum padi (L.), is a major insect pest of cereal crops in many countries. Imidacloprid has been widely used for controlling piercing-sucking insect pests worldwide, but its sublethal effects on R. padi have not been well addressed. In this study, we investigated the sublethal effects of imidacloprid on biological parameters and five enzyme activities of R. padi. The LC10, LC20, and LC25 of imidacloprid to adult aphids were 0.0053, 0.0329 and 0.0659 mg L-1, respectively. These concentrations significantly decreased pre-adult survival rate, but prolonged the development duration of 1st instar nymphs, pre-oviposition period, and adult longevity. Adult oviposition period was also extended by LC20. The intrinsic rate of increase (r), net reproductive rate (R0), and finite rate (lambda) decreased at all three concentrations, whereas mean generation time (T) increased. Moreover, LC20 and LC25 significantly inhibited superoxide dismutase (SOD) activity, but increased catalase (CAT) activity. Acetylcholinesterase (AChE) activity also increased at LC20. However, cytochrome P450 enzyme and peroxidase (POD) activity did not differ between imidacloprid treatments and the control. In conclusion, the imidacloprid concentrations tested here have negative impacts on the performance of R. padi by reducing its nymphal survival, extending the development duration of some stages, decreasing the rate of population growth, and altering enzyme activities.
ESTHER : Li_2018_PLoS.One_13_e0204097
PubMedSearch : Li_2018_PLoS.One_13_e0204097
PubMedID: 30235260

Title : Three MOF-Templated Carbon Nanocomposites for Potential Platforms of Enzyme Immobilization with Improved Electrochemical Performance - Dong_2018_ACS.Appl.Mater.Interfaces_10_14665
Author(s) : Dong S , Peng L , Wei W , Huang T
Ref : ACS Appl Mater Interfaces , 10 :14665 , 2018
Abstract : An efficient and facile metal-organic framework (MOF)-template strategy for preparing carbon nanocomposites has been developed. First of all, a series of metal ions, including Fe(3+), Zr(4+), and La(3+), were respectively connected with 2-aminoterephthalate (H2ATA) to form three metal-organic frameworks (MOFs) and then three novel MOF-derived materials were obtained by annealing them at 550 degrees C under N2 atmosphere. The morphologies and microstructure results showed that they still retained the original structure of MOFs and formed carbon-supported metal oxide hybrid nanomaterials. Interestingly, it was found that La-MOF-NH2 and its derived materials were first reported, which had wool-ball-like structure formed by many streaky-shaped particles intertwining each other. Furthermore, these MOF-derived materials were all successfully used as effective immobilization matrixes of acetylcholinesterase (AChE) to construct biosensors for the detection of methyl parathion. Especially, [La-MOF-NH2]N2 with wool-ball-like structure not only provided more active sites of multicontents to increase AChE immobilization amount but also facilitated the accessibility of electron transfer and shorten their diffusion length on the surface of electrode. Under optimal conditions, the biosensor based on [La-MOF-NH2]N2 displayed the widest linear range of 1.0 x 10(-13)-5.0 x 10(-9) g mL(-1) and the lowest detection limit of 5.8 x 10(-14) g mL(-1) in three biosensors. This study illustrates the feasibility and the potential of a series of MOF-derived materials for biosensors with improved electrochemical performance.
ESTHER : Dong_2018_ACS.Appl.Mater.Interfaces_10_14665
PubMedSearch : Dong_2018_ACS.Appl.Mater.Interfaces_10_14665
PubMedID: 29620852

Title : Synthesis of reticulated hollow spheres structure NiCo2S4 and its application in organophosphate pesticides biosensor - Peng_2017_Biosens.Bioelectron_92_563
Author(s) : Peng L , Dong S , Wei W , Yuan X , Huang T
Ref : Biosensors & Bioelectronics , 92 :563 , 2017
Abstract : Electrode materials play a key role in the development of electrochemical sensors, particularly enzyme-based biosensors. Here, a novel NiCo2S4 with reticulated hollow spheres assembled from rod-like structures was prepared by a one-pot solvothermal method and its formation mechanism was discussed. Moreover, comparison of NiCo2S4 materials from different experiment conditions as biosensors was investigated by electrochemical impedance spectroscopy (EIS) and differential pulse voltammetry (DPV), and the best one that was reticulated hollow spheres assembled from rod-like structures NiCo2S4 has been successfully employed as a matrix of AChE immobilization for the special structure, superior conductivity and rich reaction active sites. When using common two kinds of organophosphate pesticides (OPs) as model analyte, the biosensors demonstrated a wide linear range of 1.0x10-12-1.0x10-8gmL-1 with the detection limit of 4.2x10-13gmL-1 for methyl parathion, and 1.0x10-13-1.0x10-10gmL-1 with the detection limit of 3.5x10-14gmL-1 for paraoxon, respectively. The proposed biosensors exhibited many advantages such as acceptable stability and low cost, providing a promising tool for analysis of OPs.
ESTHER : Peng_2017_Biosens.Bioelectron_92_563
PubMedSearch : Peng_2017_Biosens.Bioelectron_92_563
PubMedID: 27836591

Title : Exonuclease I-aided homogeneous electrochemical strategy for organophosphorus pesticide detection based on enzyme inhibition integrated with a DNA conformational switch - Wang_2016_Analyst_141_1830
Author(s) : Wang X , Dong S , Hou T , Liu L , Liu X , Li F
Ref : Analyst , 141 :1830 , 2016
Abstract : A novel enzyme inhibition-based homogeneous electrochemical biosensing strategy was designed for an organophosphorus pesticide assay based on exploiting the resistance of a mercury ion-mediated helper probe (HP) toward nuclease-catalyzed digestion and the remarkable diffusivity difference between HPs and the mononucleotides toward a negatively charged indium tin oxide (ITO) electrode. In particular, the mercury ion-mediated T-Hg(2+)-T base pairs facilitate the HP labeled with methylene blue (MB) to fold into a hairpin structure, preventing its digestion by exonuclease I, and thus resulting in a low electrochemical response because of the large electrostatic repulsion between the negatively charged ITO electrode and the HPs. The competitive binding by a thiol group (-SH), produced in the hydrolysis reaction of acetylthiocholine (ACh) chloride with acetylcholinesterase (AChE), removes mercury ions from the base pairs, causing a nuclease-catalyzed digestion, and the subsequent electrochemical response increase due to the weak electrostatic repulsion between the product-mononucleotides and the ITO electrode. Mercury ion-mediated HPs were first designed for pesticide detection and diazinon was chosen as the model target. Under the optimal experimental conditions, the approach exhibited high sensitivity for diazinon detection with a detection limit of 0.25 mug L(-1). The satisfactory results in the determination of diazinon in real samples demonstrate that the method possesses great potential for detecting organophosphorus pesticides. This new approach is expected to promote the exploitation of mercury-mediated base pair-based homogenous electrochemical biosensors in biochemical studies and in the food safety field.
ESTHER : Wang_2016_Analyst_141_1830
PubMedSearch : Wang_2016_Analyst_141_1830
PubMedID: 26839920

Title : Fluorescence biosensing strategy based on mercury ion-mediated DNA conformational switch and nicking enzyme-assisted cycling amplification for highly sensitive detection of carbamate pesticide - Wang_2015_Biosens.Bioelectron_77_644
Author(s) : Wang X , Hou T , Dong S , Liu X , Li F
Ref : Biosensors & Bioelectronics , 77 :644 , 2015
Abstract : Pesticides are of great importance in agricultural and biological fields, but pesticide residues may harm the environment and human health. A highly sensitive fluorescent biosensor for the detection of carbamate pesticide has been developed based on acetylcholinesterase (AChE)-catalyzed hydrolysis product triggered Hg2+ release coupled with subsequent nicking enzyme-induced cleavage of a duplex DNA for cycling amplification. In this protocol, two DNA probes, an unmodified single-stranded helper DNA probe 1 (HP1) and a quencher-fluorophore probe (QFP) are ingeniously designed. HP1 can be folded into hairpin configuration through T-Hg2+-T base pair formation. QFP, labeled with FAM and BHQ1 at its two terminals, contains the recognition sequence and the cleavage site of the nicking enzyme. In the presence of carbamate pesticide, the activity of AChE is inhibited, and the amount of the product containing the thiol group generated by the hydrolysis reaction of acetylthiocholine chloride (ACh) decreases, resulting in the release of a low concentration of Hg2+. The number of HP1 that can be selectively unfolded would be reduced and the subsequent nicking enzyme-assisted cleavage processes would be affected, resulting in decreased fluorescence signals. The fluorescence intensity further decreases with the increase of the pesticide concentration. Therefore, the pesticide content can be easily obtained by monitoring the fluorescence signal change, which is inversely proportional to the logarithm of the pesticide concentration. The detection limit of aldicarb, the model analyte, is 3.3mugL-1, which is much lower than the Chinese National Standards or those previously reported. The as-proposed method has also been applied to detect carbamate pesticide residues in fresh ginger and artificial lake water samples with satisfactory results, which demonstrates that the method has great potential for practical application in biological or food safety field.
ESTHER : Wang_2015_Biosens.Bioelectron_77_644
PubMedSearch : Wang_2015_Biosens.Bioelectron_77_644
PubMedID: 26492468

Title : Synthesis and potent inhibitory activities of carboxybenzyl-substituted 8-(3-(R)-aminopiperidin-1-yl)-7-(2-chloro\/cyanobenzyl)-3-methyl-3,7-dihydro-purin e-2,6-diones as dipeptidyl peptidase IV (DPP-IV) inhibitors - Mo_2015_Bioorg.Med.Chem.Lett_25_1872
Author(s) : Mo DW , Dong S , Sun H , Chen JS , Pang JX , Xi BM , Chen WH
Ref : Bioorganic & Medicinal Chemistry Lett , 25 :1872 , 2015
Abstract : Fourteen 3-methyl-3,7-dihydro-purine-2,6-dione derivatives 1-14 bearing carboxybenzyl and 2-chloro/cyanobenzyl groups at the N-1 and N-7 positions, respectively, were synthesized as dipeptidyl peptidase IV (DPP-IV) inhibitors. These compounds were characterized on the basis of NMR ((1)H and (13)C) and ESI MS data. In vitro bioassay indicates that most of these compounds showed moderate to good inhibitory activities against DPP-IV. Among them, compound 13 (IC50=36nM) exhibited comparable activity with a positive control, Sitagliptin (IC50=16nM). In addition, the structure-activity relationship of these compounds is also briefly discussed.
ESTHER : Mo_2015_Bioorg.Med.Chem.Lett_25_1872
PubMedSearch : Mo_2015_Bioorg.Med.Chem.Lett_25_1872
PubMedID: 25838146

Title : Molecular Interactions between (-)-Epigallocatechin Gallate Analogs and Pancreatic Lipase - Wang_2014_PLoS.One_9_e111143
Author(s) : Wang S , Sun Z , Dong S , Liu Y
Ref : PLoS ONE , 9 :e111143 , 2014
Abstract : The molecular interactions between pancreatic lipase (PL) and four tea polyphenols (EGCG analogs), like (-)-epigallocatechin gallate (EGCG), (-)-gallocatechin gallate (GCG), (-)-epicatechin gallate (ECG), and (-)-epigallocatechin (EC), were studied from PL activity, conformation, kinetics and thermodynamics. It was observed that EGCG analogs inhibited PL activity, and their inhibitory rates decreased by the order of EGCG>GCG>ECG>EC. PL activity at first decreased rapidly and then slowly with the increase of EGCG analogs concentrations. alpha-Helix content of PL secondary structure decreased dependent on EGCG analogs concentration by the order of EGCG>GCG>ECG>EC. EGCG, ECG, and EC could quench PL fluorescence both dynamically and statically, while GCG only quenched statically. EGCG analogs would induce PL self-assembly into complexes and the hydrodynamic radii of the complexes possessed a close relationship with the inhibitory rates. Kinetics analysis showed that EGCG analogs non-competitively inhibited PL activity and did not bind to PL catalytic site. DSC measurement revealed that EGCG analogs decreased the transition midpoint temperature of PL enzyme, suggesting that these compounds reduced PL enzyme thermostability. In vitro renaturation through urea solution indicated that interactions between PL and EGCG analogs were weak and non-covalent.
ESTHER : Wang_2014_PLoS.One_9_e111143
PubMedSearch : Wang_2014_PLoS.One_9_e111143
PubMedID: 25365042

Title : Signatures of adaptation to obligate biotrophy in the Hyaloperonospora arabidopsidis genome - Baxter_2010_Science_330_1549
Author(s) : Baxter L , Tripathy S , Ishaque N , Boot N , Cabral A , Kemen E , Thines M , Ah-Fong A , Anderson R , Badejoko W , Bittner-Eddy P , Boore JL , Chibucos MC , Coates M , Dehal P , Delehaunty K , Dong S , Downton P , Dumas B , Fabro G , Fronick C , Fuerstenberg SI , Fulton L , Gaulin E , Govers F , Hughes L , Humphray S , Jiang RH , Judelson H , Kamoun S , Kyung K , Meijer H , Minx P , Morris P , Nelson J , Phuntumart V , Qutob D , Rehmany A , Rougon-Cardoso A , Ryden P , Torto-Alalibo T , Studholme D , Wang Y , Win J , Wood J , Clifton SW , Rogers J , Van den Ackerveken G , Jones JD , McDowell JM , Beynon J , Tyler BM
Ref : Science , 330 :1549 , 2010
Abstract : Many oomycete and fungal plant pathogens are obligate biotrophs, which extract nutrients only from living plant tissue and cannot grow apart from their hosts. Although these pathogens cause substantial crop losses, little is known about the molecular basis or evolution of obligate biotrophy. Here, we report the genome sequence of the oomycete Hyaloperonospora arabidopsidis (Hpa), an obligate biotroph and natural pathogen of Arabidopsis thaliana. In comparison with genomes of related, hemibiotrophic Phytophthora species, the Hpa genome exhibits dramatic reductions in genes encoding (i) RXLR effectors and other secreted pathogenicity proteins, (ii) enzymes for assimilation of inorganic nitrogen and sulfur, and (iii) proteins associated with zoospore formation and motility. These attributes comprise a genomic signature of evolution toward obligate biotrophy.
ESTHER : Baxter_2010_Science_330_1549
PubMedSearch : Baxter_2010_Science_330_1549
PubMedID: 21148394
Gene_locus related to this paper: hyaae-m4b4d8 , hyaae-m4b4e0 , hyaae-m4bkr1 , hyaae-m4bkw7

Title : Single-wall carbon nanotube-based voltammetric sensor and biosensor - Xu_2004_Biosens.Bioelectron_20_579
Author(s) : Xu Z , Chen X , Qu X , Jia J , Dong S
Ref : Biosensors & Bioelectronics , 20 :579 , 2004
Abstract : The pH-sensitive property of the single-wall carbon nanotube modified electrode based on the electroactive group on the single-wall carbon nanotube was explored by differential pulse voltammetry technique. In pH range 1-13 investigated in Britton-Robinson (B-R) buffer, the anodic peak shifted negatively along with the increase of pH exhibiting a reversible Nernstian response. Experiments were carried out to investigate the response of the single-wall carbon nanotube (SWNT) modified electrode to analytes associated with pH change. The response behavior of the modified electrode to ammonia was studied as an example. The potential response could reach equilibrium within 5 min. The modified electrode had good operational stability. Voltammetric urease and acetylcholinesterase biosensors were constructed by immobilizing the enzymes with sol-gel hybrid material. The maximum potential shift could reach 0.130 and 0.220 V for urea and acetylthiocholine, respectively. The methods for preparing sensor and biosensor were simple and reproducible and the range of analytes could be extended to substrates of other hydrolyases and esterases. This broadened the biosensor application of carbon nanotube in electrochemical area.
ESTHER : Xu_2004_Biosens.Bioelectron_20_579
PubMedSearch : Xu_2004_Biosens.Bioelectron_20_579
PubMedID: 15494242