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学者姓名：袁彩
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Abstract ：
Vascular thiol isomerases (VTIs) encompass proteins such as protein disulfide isomerase (PDI), endoplasmic reticulum protein 5 (ERp5), ERp46, ERp57, ERp72, thioredoxin-related transmembrane protein 1 (TMX1), and TMX4, and play pivotal functions in platelet aggregation and formation of thrombosis. Investigating vascular thiol isomerases, their substrates implicated in thrombosis, the underlying regulatory mechanisms, and the development of inhibitors targeting these enzymes represents a rapidly advancing frontier within vascular biology. In this review, we summarize the structural characteristics and functional attributes of VTIs, describe the associations between these enzymes and thrombosis, and outline the progress in developing inhibitors of VTIs for potential antithrombotic therapeutic applications.
Keyword ：
Functions Functions Inhibitors Inhibitors Structures Structures Thrombosis Thrombosis Vascular thiol isomerase Vascular thiol isomerase
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| GB/T 7714 | Jiang, Longguang , Yuan, Cai , Flaumenhaft, Robert et al. Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development [J]. | THROMBOSIS JOURNAL , 2025 , 23 (1) . |
| MLA | Jiang, Longguang et al. "Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development" . | THROMBOSIS JOURNAL 23 . 1 (2025) . |
| APA | Jiang, Longguang , Yuan, Cai , Flaumenhaft, Robert , Huang, Mingdong . Recent advances in vascular thiol isomerases: insights into structures, functions in thrombosis and antithrombotic inhibitor development . | THROMBOSIS JOURNAL , 2025 , 23 (1) . |
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Human heavy-chain ferritin (HFn) possesses a stable and uniform cage-like structure, tumor-targeting properties, self-assembly capabilities, and biocompatibility, rendering it an ideal candidate for drug delivery. Here, we developed a dual modified HFn-based nanocage (DFn) that targets the urokinase-type plasminogen activator receptor (uPAR) and, at the same time, is responsive to the tumor microenvironment for controlled extracellular drug release. This DFn was used to co-encapsulate a photosensitizer (CPZ) and a hypoxia-activated prodrug (TPZ), creating the multifunctional nanoparticles C/T@DFn. In vitro cellular assays demonstrated that C/T@DFn significantly outperformed both unmodified HFn-based nanoparticles and its counterpart without the uPARtargeting motif in inhibiting tumor cell survival, proliferation, and migration, and showed enhanced tumor cell spheroids penetration. In vivo studies further demonstrated the improved tumor-specific accumulation and antitumor efficacy of the loaded cargo in the DFn nanocages in comparison with wild-type HFn. This improved therapeutic effect is achieved through receptor-mediated targeting and tumor microenvironment-responsive release of the cargo from the DFn nanocages, resulting in synergistic action of CPZ and TPZ within the tumor tissue. Overall, this study introduces an ideal ferritin-based nanoplatform for the efficient co-delivery of therapeutic agents, offering a promising strategy for targeted tumor therapy.
Keyword ：
Antitumor Antitumor Ferritin nanocage Ferritin nanocage uPAR-targeting uPAR-targeting
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| GB/T 7714 | Li, Hanlin , Qu, Yuhan , Guo, Zhanzhi et al. Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 303 . |
| MLA | Li, Hanlin et al. "Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 303 (2025) . |
| APA | Li, Hanlin , Qu, Yuhan , Guo, Zhanzhi , Chen, Dan , Jiang, Longguang , Xu, Peng et al. Dual modified ferritin nanocages for tumor-targeted and microenvironment-responsive drug delivery . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 303 . |
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Angiogenesis provides essential nutrients and oxygen to tumors during tumorigenesis, facilitating invasion and metastasis. Consequently, inhibiting tumor angiogenesis is an established strategy in anti-cancer therapy. In this study, we engineered a dual-function nanosystem with both antiangiogenic and photodynamic properties. We transformed the hydrophobic photosensitizer zinc phthalocyanine (PS) into a hydrophilic form via protein renaturation, resulting in a novel photosensitizer: Monocyte-Activating Polypeptide-II (EMAP-II:PS@NPs). Characterization through dynamic light scattering (DLS) and UV-vis spectroscopy showed that these nano- particles exhibited uniform size and stability, and enhanced solubility. We further demonstrated that EMAP-II: PS@NPs effectively target tumor vascular endothelia causing intracellular photodynamic cytotoxicity. Notably, EMAP-II:PS@NPs achieved effective ablation of solid tumors at significantly reduced dosages of drugs compared to conventional therapies, due to their potent apoptotic effects on light-exposed cells. This study highlights the potential of combining anti-angiogenic activity with phototherapy, paving the way for innovative cancer treatment strategies.
Keyword ：
Angiogenesis Angiogenesis Anti-tumor Anti-tumor EMAP-II EMAP-II Phthalocyanine Phthalocyanine
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| GB/T 7714 | Chen, Liyun , Li, Linlin , Zhao, Hailong et al. Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment [J]. | COLLOIDS AND SURFACES B-BIOINTERFACES , 2025 , 248 . |
| MLA | Chen, Liyun et al. "Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment" . | COLLOIDS AND SURFACES B-BIOINTERFACES 248 (2025) . |
| APA | Chen, Liyun , Li, Linlin , Zhao, Hailong , Li, Hao , Li, Jiahui , Li, Chao et al. Integration of EMAP-II-targeted anti-angiogenesis and photodynamic therapy using zinc phthalocyanine nanosystem for enhanced cancer treatment . | COLLOIDS AND SURFACES B-BIOINTERFACES , 2025 , 248 . |
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The angiopoietin (Ang)-Tie axis, critical for endothelial cell function and vascular development, is a promising therapeutic target for treating vascular disorders and inflammatory conditions like sepsis. This study aimed to enhance the binding affinity of recombinant Ang1 variants to the Tie2 and explore their therapeutic potential. Structural insights from the Ang1-Tie2 complex enabled the identification of key residues within the Ang1 receptor binding domain (RBD) critical for Tie2 interaction. Molecular dynamics simulations revealed that Met436Arg (M436R) and Ala451Asp (A451D) could improve Ang1's Tie2 binding affinity. One variant, Ang1-RBDA451D, demonstrated a 100-fold increase compared to the wild type. Cellular assays revealed that Ang1A451D enhanced Tie2 phosphorylation, promoting endothelial cell migration and tube formation. In vivo, this variant effectively reduced inflammatory cytokines and attenuated organ damage in septic mice. These findings highlight Ang1A451D as a promising therapeutic candidate for vascular diseases, offering notable clinical potential for mitigating sepsis-related vascular dysfunction.
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| GB/T 7714 | Wang, Rui , Li, Hao , Xie, Zhinuo et al. Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice [J]. | SCIENCE ADVANCES , 2025 , 11 (3) . |
| MLA | Wang, Rui et al. "Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice" . | SCIENCE ADVANCES 11 . 3 (2025) . |
| APA | Wang, Rui , Li, Hao , Xie, Zhinuo , Huang, Meijuan , Xu, Peng , Yuan, Cai et al. Development of a recombinant Ang1 variant with enhanced Tie2 binding and its application to attenuate sepsis in mice . | SCIENCE ADVANCES , 2025 , 11 (3) . |
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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.
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, Haili , Xu, Mingming , Jiang, Longguang et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue [J]. | BIOORGANIC CHEMISTRY , 2024 , 152 . |
| MLA | Lin, Haili et al. "Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue" . | BIOORGANIC CHEMISTRY 152 (2024) . |
| APA | Lin, Haili , Xu, Mingming , Jiang, Longguang , Yuan, Cai , Jiang, Chuan , Huang, Mingdong et al. Water-medicated specifically targeting the S1 pockets among serine proteases using an arginine analogue . | BIOORGANIC CHEMISTRY , 2024 , 152 . |
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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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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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In the type III CRISPR system, cyclic oligoadenylate (cOA) molecules act as second messengers, activating various promiscuous ancillary nucleases that indiscriminately degrade host and viral DNA/RNA. Conversely, ring nucleases, by specifically cleaving cOA molecules, function as off-switches to protect host cells from dormancy or death, and allow viruses to counteract immune responses. The fusion protein Csx1-Crn2, combining host ribonuclease with viral ring nuclease, represents a unique self-limiting ribonuclease family. Here, we describe the structures of Csx1-Crn2 from the organism of Marinitoga sp., in both its full-length and truncated forms, as well as in complex with cA4. We show that Csx1-Crn2 operates as a homo-tetramer, a configuration crucial for preserving the structural integrity of the HEPN domain and ensuring effective ssRNA cleavage. The binding of cA4 to the CARF domain triggers significant conformational changes across the CARF, HTH, and into the HEPN domains, leading the two R-X4-6-H motifs to form a composite catalytic site. Intriguingly, an acetate ion was found to bind at this composite site by mimicking the scissile phosphate. Further molecular docking analysis reveals that the HEPN domain can accommodate a single ssRNA molecule involving both R-X4-6-H motifs, underscoring the importance of HEPN domain dimerization for its activation. Graphical Abstract
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| GB/T 7714 | Zhang, Danping , Du, Liyang , Gao, Haishan et al. Structural insight into the Csx1-Crn2 fusion self-limiting ribonuclease of type III CRISPR system [J]. | NUCLEIC ACIDS RESEARCH , 2024 , 52 (14) : 8419-8430 . |
| MLA | Zhang, Danping et al. "Structural insight into the Csx1-Crn2 fusion self-limiting ribonuclease of type III CRISPR system" . | NUCLEIC ACIDS RESEARCH 52 . 14 (2024) : 8419-8430 . |
| APA | Zhang, Danping , Du, Liyang , Gao, Haishan , Yuan, Cai , Lin, Zhonghui . Structural insight into the Csx1-Crn2 fusion self-limiting ribonuclease of type III CRISPR system . | NUCLEIC ACIDS RESEARCH , 2024 , 52 (14) , 8419-8430 . |
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