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学者姓名：江龙光
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Abstract ：
Serine proteases, a significant class of enzymes comprising approximately one-third of known human proteases, are ubiquitously present across various organisms. These enzymes typically exhibit highly conserved catalytic domain structures, and their activity is stringently regulated within the body, playing a pivotal role in numerous physiological processes. Dysregulation of serine protease activity can result in severe consequences, including excessive inflammation, heightened risk of thrombosis and cancer, and even mortality. Serine protease inhibitors have emerged as critical regulators, offering a broad range of physiological functions such as maintaining the coagulation-fibrinolysis balance, modulating inflammatory responses, accelerating wound healing, promoting apoptosis, and providing antitumor and antiviral effects. As a result, the development of serine protease inhibitors has become increasingly vital. In recent years, significant progress in the study of serine proteases has led to the pivotal role of various serine protease inhibitors in clinical diagnosis and treatment. This review explores the fundamental mechanisms of serine protease inhibitors, summarizes those that have been successfully integrated into clinical practice, and discusses the challenges encountered in their development along with partial solutions. These advancements lay the groundwork for further refinement and innovation in serine protease inhibitor therapeutics.
Keyword ：
challenges challenges clinical application clinical application serine protease serine protease serine protease inhibitor serine protease inhibitor strategies strategies
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| GB/T 7714 | Wei, Yang , Huang, Mingdong , Jiang, Longguang . Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications [J]. | CATALYSTS , 2024 , 14 (11) . |
| MLA | Wei, Yang 等. "Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications" . | CATALYSTS 14 . 11 (2024) . |
| APA | Wei, Yang , Huang, Mingdong , Jiang, Longguang . Advancements in Serine Protease Inhibitors: From Mechanistic Insights to Clinical Applications . | CATALYSTS , 2024 , 14 (11) . |
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The global epidemic of COVID-19 has intensified the urgency for the development of high-efficiency air filters with antiviral and antibacterial properties. While conventional commercial air purifiers can filter particulate matter, they often fall short of eradicating airborne pathogens. Thus, there is a critical need to innovate air filtration systems capable of not just trapping but exterminating harmful microorganisms to impede their airborne transmission. One potential solution is to use antibacterial photodynamic technique (aPDT). Indeed, recent years have witnessed the rapid growth in this area. This review summaries applications of aPDT for air disinfection through the inactivation of bacteria, fungi, and viruses. In addition, the mechanisms of photosensitizer-assisted pathogen inactivation and the futher development in photodynamic air disinfection technique are also discussed.
Keyword ：
Airborne pathogens Airborne pathogens Antibacterial photodynamic therapy Antibacterial photodynamic therapy Antimicrobial filter Antimicrobial filter Photosensitizers Photosensitizers
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| GB/T 7714 | Lin, Yuxin , Chen, Liyun , Jiang, Longguang et al. Recent advances in filter materials for efficient photodynamic inactivation of pathogens in the air [J]. | JOURNAL OF ENVIRONMENTAL CHEMICAL ENGINEERING , 2024 , 12 (6) . |
| MLA | Lin, Yuxin et al. "Recent advances in filter materials for efficient photodynamic inactivation of pathogens in the air" . | JOURNAL OF ENVIRONMENTAL CHEMICAL ENGINEERING 12 . 6 (2024) . |
| APA | Lin, Yuxin , Chen, Liyun , Jiang, Longguang , Huang, Mingdong . Recent advances in filter materials for efficient photodynamic inactivation of pathogens in the air . | JOURNAL OF ENVIRONMENTAL CHEMICAL ENGINEERING , 2024 , 12 (6) . |
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In recent years, immunization with the S2 live-attenuated vaccine has been recognized as the most economical and effective strategy for preventing brucellosis in Inner Mongolia, China. However, there are still challenges related to vaccine toxicity and the inability to distinguish between vaccine immunization and natural infection. Therefore, in this study, we developed a digital droplet polymerase chain reaction (ddPCR) assay based on single-nucleotide polymorphism (SNP) loci to identify wild Brucella strains and S2 vaccine strains. The assay demonstrated excellent linearity (R2> 0.99) with a lower detection limit of 10 copies/µL for both wild and vaccine strains. Additionally, the ddPCR assay outperformed the real-time fluorescent quantitative PCR (qPCR) assay in screening 50 clinical samples. We have established an effective and highly sensitive ddPCR assay for Brucella, providing an efficient method for detecting and differentiating wild strains of Brucella from the S2 vaccine strain. © 2024 The Author(s)
Keyword ：
Brucella Brucella Digital droplet polymerase chain reaction Digital droplet polymerase chain reaction S2 Vaccine strain S2 Vaccine strain Single-nucleotide polymorphism Single-nucleotide polymorphism Wild strains Wild strains
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| GB/T 7714 | Li, W. , Zhang, S. , Dang, S. et al. Establishment of an A/T-Rich Specifically MGB Probe digital droplet PCR Assays Based on SNP for Brucella wild strains and vaccine strains [J]. | Diagnostic Microbiology and Infectious Disease , 2024 , 110 (1) . |
| MLA | Li, W. et al. "Establishment of an A/T-Rich Specifically MGB Probe digital droplet PCR Assays Based on SNP for Brucella wild strains and vaccine strains" . | Diagnostic Microbiology and Infectious Disease 110 . 1 (2024) . |
| APA | Li, W. , Zhang, S. , Dang, S. , Gao, L. , Li, G. , Cheng, D. et al. Establishment of an A/T-Rich Specifically MGB Probe digital droplet PCR Assays Based on SNP for Brucella wild strains and vaccine strains . | Diagnostic Microbiology and Infectious Disease , 2024 , 110 (1) . |
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Aims Alteplase is a cornerstone thrombolytic agent in clinical practice but presents a potential bleeding risk. Stroke patients need pre-screening to exclude haemorrhagic stroke before using alteplase. In this study, we develop a new thrombolytic agent citPA5, characterized by an enhanced safety profile and minimal bleeding tendency.Methods and results A clot lysis agent, named citPA5, is developed based on rtPA with point mutations to completely suppress its proteolytic activity in the absence of fibrin. In the presence of fibrin, citPA5 exhibited significantly higher fibrinolytic activity (a 15.8-fold increase of kcat/Km). Furthermore, citPA5 showed resistance to endogenous fibrinolysis inhibitor, PAI-1, resulting in enhanced potency. In a series of safety evaluation experiments, including thrombelastography assay, mice tail bleeding assay, and a murine intracerebral haemorrhage (ICH) model, citPA5 did not cause systemic bleeding or worsen ICH compared with alteplase. This highlights the low risk of bleeding associated with citPA5. Finally, we found that citPA5 effectively improved cerebral blood flow and reduced infarct volume in a carotid embolism-induced stroke model.Conclusion This clot lysis agent, citPA5, not only exhibits a low risk of bleeding but also demonstrates highly effective thrombolysis capabilities. As a result, citPA5 shows great potential for administration prior to the classification of stroke types, making it possible for use in ambulances at the onset of stroke when symptoms are identified. The findings presented in this study also suggest that this strategy could be applied to develop a new generation of fibrinolytic drugs that offer greater safety and specificity in targeting fibrin. Graphical Abstract
Keyword ：
Enhanced tPA potency Enhanced tPA potency Ischaemic stroke Ischaemic stroke Low bleeding risk Low bleeding risk Thrombolytic therapy Thrombolytic therapy
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| GB/T 7714 | Chen, Shanli , Fang, Sudan , Zhou, Yang et al. A low bleeding risk thrombolytic agent: citPA5 [J]. | CARDIOVASCULAR RESEARCH , 2024 , 120 (10) : 1191-1201 . |
| MLA | Chen, Shanli et al. "A low bleeding risk thrombolytic agent: citPA5" . | CARDIOVASCULAR RESEARCH 120 . 10 (2024) : 1191-1201 . |
| APA | Chen, Shanli , Fang, Sudan , Zhou, Yang , Huang, Zhiwei , Yu, Shujuan , Chen, Dan et al. A low bleeding risk thrombolytic agent: citPA5 . | CARDIOVASCULAR RESEARCH , 2024 , 120 (10) , 1191-1201 . |
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Bacterial infections of plants are widespread and highly virulent, causing serious economic losses in agricultural production worldwide. These infections become particularly prevalent during rainy weather, characterized by high humidity and low light intensity (about 2-10% of a sunny day). Here we identified a class of photosensitizers that were effective in inhibiting plant bacterial infections under rainy weather with dim light. One of these compounds, compound 1, demonstrated exceptional efficacy by eliminating more than 4 logs (99.99%) of either Xanthomonas perforans or Xanthomonas citri subsp. citri (Xcc) strain at a concentration of 6.25 mu M under rainy weather conditions with a light exposure of 28.51 J/cm2. For Clavibacter michiganensis (Cm), compound 1 demonstrated a comparable bactericidal effect at a lower concentration of 3.13 mu M. Furthermore, compound 1 was effective in controlling plant leaf infections during rainy weather. Moreover, compound 1 exhibited a potent inhibitory effect on the biofilms pertinent to tomato spot disease and citrus canker under natural illumination on rainy days. Additionally, compound 1 displayed remarkable resilience to rain-wash on plant leaves, retaining 41.20% of its initial concentration following exposure to three simulated rain events. These findings provide a new strategy for plant pathogen disease management highlight its feasibility even during rainy weather.
Keyword ：
Biofilm Biofilm Photosensitizer Photosensitizer Plant bacterial infection Plant bacterial infection Rain fastness Rain fastness
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| GB/T 7714 | Wang, Guodong , Li, Jiahui , Zhang, Wei et al. A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light [J]. | DYES AND PIGMENTS , 2024 , 225 . |
| MLA | Wang, Guodong et al. "A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light" . | DYES AND PIGMENTS 225 (2024) . |
| APA | Wang, Guodong , Li, Jiahui , Zhang, Wei , Jiang, Libin , Mai, Yuhan , Chen, Jingyi et al. A class of photosensitizer highly effective to control bacterial infection in plants even on rainy days with dim light . | DYES AND PIGMENTS , 2024 , 225 . |
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Because of the high similarity in structure and sequence, it is challenging to distinguish the S1 pocket among serine proteases, primarily due to the only variability at residue 190 (A190 and S190). Peptide or protein-based inhibitors typically target the negatively charged S1 pocket using lysine or arginine as the P1 residue, yet neither discriminates between the two S1 pocket variants. This study introduces two arginine analogues, L-4-guanidinophenylalanine (12) and L-3-(N-amidino-4-piperidyl)alanine (16), as novel P1 residues in peptide inhibitors. 16 notably enhances affinities across all tested proteases, whereas 12 specifically improved affinities towards proteases possessing S190 in the S1 pocket. By crystallography and molecular dynamics simulations, we discovered a novel mechanism involving a water exchange channel at the bottom of the S1 pocket, modulated by the variation of residue 190. Additionally, the specificity of 12 towards the S190-presenting S1 pocket is dependent on this water channel. This study not only introduces novel P1 residues to engineer inhibitory potency and specificity of peptide inhibitors targeting serine proteases, but also unveils a water-mediated molecular mechanism of targeting serine proteases. © 2024 Elsevier Inc.
Keyword ：
P1 residue P1 residue Peptide inhibitors Peptide inhibitors S1 pocket S1 pocket Serine protease Serine protease Specificity Specificity
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| GB/T 7714 | Lin, H. , Xu, M. , Jiang, L. et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue [J]. | Bioorganic Chemistry , 2024 , 152 . |
| MLA | Lin, H. et al. "Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue" . | Bioorganic Chemistry 152 (2024) . |
| APA | Lin, H. , Xu, M. , Jiang, L. , Yuan, C. , Jiang, C. , Huang, M. et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue . | Bioorganic Chemistry , 2024 , 152 . |
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Background: Endothelial hyperpermeability-induced vascular dysfunction is a prevalent and significant characteristic in critical illnesses such as sepsis and other conditions marked by acute systemic inflammation. Platelet endothelial cell adhesion molecule-1 (PECAM-1) and Tie2 serve as transmembrane receptors within endothelial cells (ECs), playing pivotal roles not only in maintaining EC-EC junctions but also in influencing vasculogenesis, vessel homeostasis, and vascular remodeling. Objectives: At present, the molecular basis of the PECAM-1-Tie2 interaction remains inadequately elucidated. In the study, recombinant soluble PECAM-1 (sPECAM-1) and Tie2 (sTie2) were expressed by Drosophila S2 and HEK293 expression systems, respectively. The interactions between sPECAM-1 and sTie2 were investigated using the Surface Plasmon Resonance (SPR) and size-exclusion chromatography methods. An immunofluorescence assay was used to detect the binding of sPECAM-1 and sTie2 on endothelial cells. Results: PECAM-1 was found to bind with sTie2 in a sodium and pH-dependent manner as confirmed by the ELISA, the D5-D6 domains of PECAM-1 might play a crucial role in binding with sTie2. Surface Plasmon Resonance (SPR) results showed that the full length of sPECAM-1 has the strongest binding affinity (KD = 48.4 nM) with sTie2, compared to sPECAM-1-D1-D4 and sPECAM-1-D1-D2. This result is consistent with that in the ELISA. In addition, size-exclusion chromatography demonstrated that sPECAM-1, sTie2, and Ang1 can form a ternary complex. Conclusion: In this study, we determined that sPECAM-1 binds to sTie2 in a pH and sodium-dependent manner. The full length of sPECAM-1 has the strongest binding affinity, and the D5-D6 domains in sPECAM-1 play a crucial role in the interaction between sPECAM-1 and sTie2.
Keyword ：
Angiopoietin-1 Angiopoietin-1 Endothelial cell Endothelial cell PECAM-1 PECAM-1 Protein-protein interaction Protein-protein interaction Tie2 Tie2
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| GB/T 7714 | Li, Hao , Wang, Rui , Xu, Peng et al. Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation [J]. | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS , 2024 , 735 . |
| MLA | Li, Hao et al. "Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation" . | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 735 (2024) . |
| APA | Li, Hao , Wang, Rui , Xu, Peng , Yuan, Cai , Huang, Mingdong , Jiang, Longguang . Elucidating the molecular basis of PECAM-1 and Tie2 interaction from binding dynamics and complex formation . | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS , 2024 , 735 . |
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Human heavy chain ferritin (HFn) protein cage has been explored as a nanocarrier for targeted anticancer drug delivery. Here, we introduced a matrix metalloproteinases (MMPs)-cleavable sequence into the DE loop of HFn, creating an MMP-responsive variant, MR-HFn, for localized and extracellular drug release. The crystal structure of MR-HFn revealed that the addition of the MMPs recognition sequence did not affect the self -assembly of HFn but presented a surface -exposed loop susceptible to MMPs cleavage. Biochemical analysis indicated that this engineered protein cage is responsive to MMPs, enabling the targeted release of encapsulated drugs. To evaluate the therapeutic potential of this engineered protein cage, monosubstituted beta -carboxy phthalocyanine zinc (CPZ), a type of photosensitizer, was loaded inside this protein cage. The prepared CPZ@MR-HFn showed higher uptake and stronger phototoxicity in MMPs overexpressed tumor cells, as well as enhanced penetration into multicellular tumor spheroids compared with its counterpart CPZ@HFn in vitro. In vivo, CPZ@MR-HFn displayed a higher tumor inhibitory rate than CPZ@HFn under illumination. These results indicated that MR-HFn is a promising nanocarrier for anticancer drug delivery and the MMP-responsive strategy here can also be adapted for other stimuli.
Keyword ：
Human heavy chain ferritin Human heavy chain ferritin Localized extracellular release Localized extracellular release Tumor microenvironment responsive Tumor microenvironment responsive
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| GB/T 7714 | Yan, Wen , Li, Hanlin , Ning, Jiamin et al. Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 267 . |
| MLA | Yan, Wen et al. "Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 267 (2024) . |
| APA | Yan, Wen , Li, Hanlin , Ning, Jiamin , Huang, Shuhao , Jiang, Longguang , Xu, Peng et al. Engineered protein cages with enhanced extracellular drug release for elevated antitumor efficacy . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2024 , 267 . |
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Lysosomes are promising therapeutic targets for cancer therapy due to their essential function and increased vulnerability in cancer cells. Herein, we report a new category of cationic photosensitizers (compounds 1-3) containing a quaternary ammonium group. These photosensitizers exhibited selective uptake on cancer cells (about three times compared to the normal cells), lysosome-specific localization (Pearson's coefficients greater than 0.85), remarkable phototoxicity (IC50 are in the range of dozens of nM), and at the same time, favorable biosafety. Mechanically, these tumor-targeting photosensitizers function as light-controlled "bombs", inducing lysosomal membrane permeabilization (LMP), ultimately resulting in apoptosis of cancer cells. In vivo, compound 1 (a representative of these novel photosensitizers) accumulated predominantly in and visualized tumors implanted on mice. Upon exposure to near-infrared light irradiation (50 J/cm2), the compound effectively ablated the tumor at a low dose of 2 mg/kg. Our results demonstrate a novel class of photosensitizers showing potential for integrated cancer diagnosis and photodynamic treatment.
Keyword ：
Lysosomal membrane permeabilization Lysosomal membrane permeabilization Photodynamic therapy Photodynamic therapy Phthalocyanine Phthalocyanine Tumor-targeting Tumor-targeting
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| GB/T 7714 | Li, Jiahui , Wang, Guodong , Mai, Yuhan et al. Lysosome-localization and tumor-targeting of novel photosensitizers enhance the ablation of cancer [J]. | JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY , 2024 , 261 . |
| MLA | Li, Jiahui et al. "Lysosome-localization and tumor-targeting of novel photosensitizers enhance the ablation of cancer" . | JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY 261 (2024) . |
| APA | Li, Jiahui , Wang, Guodong , Mai, Yuhan , Zhang, Wei , Zhao, Hailong , Zhou, Yang et al. Lysosome-localization and tumor-targeting of novel photosensitizers enhance the ablation of cancer . | JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY , 2024 , 261 . |
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Diltiazem and glibenclamide are commonly used hypotensive and antidiabetic drugs. This study reports the discovery of the potential antitumor and antimetastatic effects of these two drugs using a structural dynamics-driven virtual screening targeting urokinase receptor (uPAR). Owing to uPAR's high flexibility, currently resolved crystal structures of uPAR, all in ligand-bound states, provide limited representations of its physiological conformation. To improve the accuracy of screening, we performed a long-timescale molecular dynamics simulation and obtained the representative conformations of apo-uPAR as the targets for our screening. Experimentally, we demonstrated that diltiazem and glibenclamide bound uPAR with KD values in the micromolar range. In addition, both compounds effectively suppressed tumor growth and metastasis in a uPAR-dependent manner in vitro and in vivo. This work not only provides two potent uPAR inhibitors but also reports a proof-of-concept study on the potential off-label antitumor and antimetastatic uses of diltiazem and glibenclamide.
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| GB/T 7714 | Zhou, Yang , Song, Meiru , Xie, Daoqing et al. Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor [J]. | JOURNAL OF MEDICINAL CHEMISTRY , 2023 , 66 (8) : 5415-5426 . |
| MLA | Zhou, Yang et al. "Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor" . | JOURNAL OF MEDICINAL CHEMISTRY 66 . 8 (2023) : 5415-5426 . |
| APA | Zhou, Yang , Song, Meiru , Xie, Daoqing , Yan, Shufeng , Xie, Song , Cai, Meiqin et al. Structural Dynamics-Driven Discovery of Anticancer and Antimetastatic Effects of Diltiazem and Glibenclamide Targeting Urokinase Receptor . | JOURNAL OF MEDICINAL CHEMISTRY , 2023 , 66 (8) , 5415-5426 . |
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