Nano-Micro Letters
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2025
·Vol. 18
·期 1
·62
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IF 36.3
Zheng Xiaojian,Ahmed Shehzad,Zhang Yu,Xu Guoqiang,Wang Junyu,Lu Di,Shi Tingshu,Tang Jun,Yan Lei,Chen Wei,Han Peigang,Liu Zhixin,Khan Danish,Wang Xingzhu,Tang Zeguo
Benzamidine derivatives are utilized to differentiate between 2D passivation and amorphous passivation.
Introducing an n-type 2D passivation layer enhances the charge extraction and transportation and reduces the interface recombination in inverted perovskite solar cells.
The intramolecular charge of organic ligands is critical for the formation of crystalline 2D capping layers on 3D perovskite layers.
The long-term stability of inverted perovskite solar cells is improved owing to hydrophobic sealing of 3D perovskite via crystalline 2D capping.
研究领域:
材料科学
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光伏技术
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表面化学
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半导体器件
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纳米结构材料
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PubMed
高影响因子
JOURNAL OF SEPARATION SCIENCE
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2020
·Vol. 43
·期 15
·3136-3145
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IF 2.878
Hao Zhang,Min Lu,Hui Jiang,Xu Wang,Feng-Qing Yang
In this study, a capillary electrophoresis-based online immobilized enzyme microreactor was developed for evaluating the inhibitory activity of green tea catechins and tea polyphenol extracts on trypsin. The immobilized trypsin activity and other kinetic parameters were evaluated by measuring the peak area of the hydrolyzate of chromogenic substrate S-2765. The results indicated that the activity of the immobilized trypsin remained approximately 90.0% of the initial immobilized enzyme activity after 30 runs. The value of Michaelis–Menten constant ( K m ) was (0.47 ± 0.08) mM, and the half-maximal inhibitory concentration (IC 50 ) and inhibition constant ( K i ) of benzamidine were measured as 3.34 and 3.00 mM, respectively. Then, the inhibitory activity of four main catechins (epicatechin, epigallocatechin, epicatechin gallate, and epigallocatechin gallate) and three tea polyphenol extracts (green tea, white tea, and black tea) on trypsin were investigated. The results showed that four catechins and three tea polyphenol extracts had potential trypsin inhibitory activity. In addition, molecular docking results illustrated that epigallocatechin gallate, epicatechin gallate, epicatechin, and epigallocatechin were all located not only in the catalytic cavity, but also in the substrate-binding pocket of trypsin. These results indicated that the developed method is an effective tool for evaluating inhibitory activity of catechins on trypsin.
研究领域:
分析化学
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生物化学
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药理学
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食品科学
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DOI
PubMed
高影响因子
TALANTA
·
2024
·
IF 5.6
Ya-Qi Zhao,Zhi-Peng Li,Shi-Chao Dong,Hao Wang,Yi-Mei Zhao,Lin-Yi Dong,Zhen-Yu Zhao,Xian-Hua Wang
The effective method for trypsin purification should be established because trypsin has important economic value. In this work, a novel and simple strategy was proposed for fabricating micron-sized magnetic Fe 3 O 4 @agarose-benzamidine beads (MABB) with benzamidine as a ligand, which can efficiently and selectively capture trypsin. The micro-sized MABB, with clear spherical core-shell structure and average particle size of 6.6 μm, showed excellent suspension ability and magnetic responsiveness in aqueous solution. The adsorption capacity and selectivity of MABB towards target trypsin were significantly better than those of non-target lysozyme. According to the Langmuir equation, the maximum adsorption capacity of MABB for trypsin was 1946 mg g −1 at 25 °C, and the adsorption should be a physical sorption process. Furthermore, the initial adsorption rate and half equilibrium time of MABB toward trypsin were 787.4 mg g −1 min −1 and 0.71 min, respectively. To prove the practicability, MABB-based magnetic solid-phase extraction (MSPE) was proposed, and the related parameters were optimized in detail to improve the purification efficiency. With Tris-HCl buffer (50 mM, 10 mM CaCl 2 , pH 8.0) as extraction buffer, Tris-HCl buffer (50 mM, 100 mM CaCl 2 , pH 8.0) as rinsing buffer, acidic eluent (0.01 M HCl, 0.5 M NaCl, pH 2.0) as eluent buffer and alkaline buffer (1 M Tris-HCl buffer, pH 10.0) as neutralization solution, the MABB-based MSPE was successfully used for trypsin purification from the viscera of grass carp ( Ctenopharyngodon idella ). The molecular weight of purified trypsin was determined as approximate 23 kDa through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The purified trypsin was highly active from 30 °C to 60 °C, with an optimum temperature of 50 °C, and was tolerant to pH variation, exhibiting 85 % of maximum enzyme activity from pH 7.0 to 10.0. The results demonstrated that the proposed MABB-based MSPE could effectively purify trypsin and ensure the biological activity of purified trypsin. Therefore, we believe that the novel MABB could be applicable for efficient purification of trypsin from complex biological systems.
研究领域:
生物化学
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生物技术
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分析化学
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蛋白质纯化
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酶学
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PubMed
高影响因子
JOURNAL OF HAZARDOUS MATERIALS
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2019
·
IF 7.65
Na Liu,Han Zhang,Jinfeng Zhao,Yin Xu,Fei Ge
Microalgae photosynthesis is sensitive to coexisted contaminates in aquatic environment, thereby causes adverse effect on algal growth and nutrients uptake. Here, we investigated the photosynthetic toxicity mechanism of cetyltrimethyl ammonium chloride (CTAC)-induced on a green microalga Chlorella vulgaris F1068 ( C. vulgaris F1068). Results showed that CTAC reduced the algal growth rate, nutrients removal efficiency and weakened the photosynthetic performance. Meanwhile, the efficiency of oxygen evolution complex (OEC) and oxygen evolvement rates stressed by CTAC were significantly declined to 90.48% and 58.48% of the control (without CTAC), respectively. In addition, atomic force microscopy (AFM) detected the damage of PSII-OEC morphology and structure by CTAC. Furthermore, proteomic analysis showed that 41% of proteins were in the chloroplast thylakoid membranes which function in photosynthesis. The activity of oxygen-evolving enhancer protein 2 (OEE2 or PsbP) involved in electron transfer was significantly inhibited by CTAC, which down-regulated 15.14-fold in the presence of 0.6 mg/L CTAC. These results indicated that photosynthetic inhibition of CTAC mainly occurred in the PSII-OEC. This study provided a new perspective of the photosynthetic response in evaluation of environmental bioimpacts of surfactants on microalgae.
研究领域:
环境科学
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植物生理学
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高影响因子
JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE
·
2022
·Vol. 102
·期 13
·5858-5866
·
IF 4.125
Jiandong Shen,Wei Zhang,Qixing Jiang,Pei Gao,Yanshun Xu,Wenshui Xia
BACKGROUND Textural deterioration is a serious problem in chilled fish flesh. Cysteine proteinases are proposed to participate in disintegration of collagen fibers during this process, while its mechanism remains elusive. In the present study, a cysteine proteinase was purified from grass carp muscle and identified by mass spectrometry, and its effect on structural changes of collagen fibers was investigated. RESULTS During storage at 4 °C, cysteine proteinase activity in fillets increased to 1.53-fold at day 5 and maintained a high level later, and this variable was related to a decline in shear force and an increase in drip loss. A 29 kDa cysteine proteinase was purified through ammonium sulfate precipitation and column chromatography, and identified as cathepsin L. Cathepsin L caused collagen fibers to partly disintegrate into fibril bundles and individual fibrils at 48 h, while the triple helical structure of collagen molecules remained stable. Release of soluble proteins and glycosaminoglycans from cathepsin L-treated collagen fibers was time dependent, coinciding with a release of 4.12 ± 0.13% and 8.57 ± 0.03% at 48 h respectively. However, 0.85 ± 0.02% of hydroxyproline was freed from cathepsin L-treated collagen fibers at 48 h. Furthermore, scanning electron microscopy revealed that the inhibitory effect of cathepsin L could retard the destruction of intramuscular connective tissues (IMCTs). CONCLUSION These results indicated that cathepsin L might be involved in collagen fiber breakdown by degrading collagen-associated proteoglycans during textural deterioration of grass carp. © 2022 Society of Chemical Industry.
研究领域:
食品科学
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生物化学
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水产养殖
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PubMed
高影响因子
ANALYTICAL LETTERS
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2022
·
IF 2.267
Ru Li,Xuan Zou,Pan Luan,Xiaokun Liu,Ning Wang,Qian Wang,Huashi Guan,Zhe Xu
Thrombosis is the main cause of many cardiovascular diseases. The conventional pharmaceuticals used for preventing thrombosis can induce significant adverse side effects, especially bleeding risk. Hence, the development of more effective and safe antithrombotic agents is strongly demanded to improve clinical treatment. In order to rapidly screen and identify novel antithrombotic substances from natural marine products, a multi-target screening strategy is reported to quantify the antithrombotic activity with high-performance liquid chromatography – mass spectrometry (HPLC-MS). Five key thrombosis-related targets, including thrombin, coagulation factors Xa, XIa and XIIa and platelet phosphodiesterase 3, were selected to establish the multi-target antithrombotic activity screening assay. The Michaelis-Menten constants (Km) were 8.16 µM, 58.85 µM, 120.03 µM, 35.24 µM and 79.67 µM, respectively. Five known inhibitors, namely argatroban, rivaroxaban, benzamidine, 3-carboxamide-coumarinand, and milrinone, were used for validation. The reproducibility of the screening strategy was verified by calculating the overall average Z′ value, which was 0.88. Subsequently, this method was assessed by screening a small marine library of 78 compounds. Five coumarin compounds were selected, and their antithrombotic activities were further validated in standard assessments of enzyme inhibition and on the coagulometer. According to the validation, the multi-target assay based on dried blood spots and HPLC-MS was suitable for screening antithrombotic substances with considerable reliability.
研究领域:
药理学
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分析化学
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心血管病学
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高影响因子
危险品化学品经营许可证（带存储）