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学者姓名：袁彩
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Abstract ：
Diabetic wounds complicated by bacterial infections present a significant clinical challenge, and cause a great burden to the world's health care systems. Infections by bacteria, especially drug-resistant bacteria, is the major underlying factor leading to diabetic wounds. Here, we synthesized a series of fluoroborane dipyrrole compounds that can be activated under ambient light conditions, and identified one compound with potent antibacterial action. The compound has a maximum absorption wavelength of 538 nm, close to the maximum emission wavelength of sunlight, making it particularly suitable for incorporation into transparent antimicrobial patches. We fabricated such a patch and evaluated its therapeutic potential in a murine model of diabetic wounds infected with drug-resistant bacteria. The experimental results showed that the patch not only eradicates drug-resistant bacterial strains but also promoted wound healing under ambient light. Furthermore, the compound exhibited a high level of biosafety. This work developed an effective and safe method to combat bacterial skin infections associated with diabetic wounds.
Keyword ：
Antimicrobial photodynamic therapy Antimicrobial photodynamic therapy BODIPY BODIPY Diabetic wounds Diabetic wounds Drug-resistant bacteria Drug-resistant bacteria Photosensitizer Photosensitizer Transparent patches Transparent patches
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| GB/T 7714 | Deng, Lina , Chen, Zheng , Jiang, Libin et al. Treatment of diabetic infection wounds using novel fluoroborane dipyrrole-coated transparent patch [J]. | BIOORGANIC CHEMISTRY , 2025 , 163 . |
| MLA | Deng, Lina et al. "Treatment of diabetic infection wounds using novel fluoroborane dipyrrole-coated transparent patch" . | BIOORGANIC CHEMISTRY 163 (2025) . |
| APA | Deng, Lina , Chen, Zheng , Jiang, Libin , Jing, Qian , Wang, Shuai , Yang, De-Chao et al. Treatment of diabetic infection wounds using novel fluoroborane dipyrrole-coated transparent patch . | BIOORGANIC CHEMISTRY , 2025 , 163 . |
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Sporulation factor IV B protease (SpoIVB), as a PDZ-protease, plays a central role in cellular differentiation via activating pro-sigma K processing at the sigma K checkpoint during spore formation. However, the molecular mechanism and structure of SpoIVB remain unclear. In this study, we expressed and characterized several recombinant variants of SpoIVB, including SpoIVB75-426, SpoIVB75-426-S378A, and SpoIVB101-426-S378A. Their structural properties were analyzed through dynamic light scattering, size-exclusion chromatography, small-angle X-ray scattering (SAXS), and X-ray crystallography. The crystal structure of SpoIVB101-426-S378A was determined at 2.49 & Aring; resolution, revealing a unique PDZ domain arrangement and an unusual catalytic triad in the serine protease domain. SAXS analysis demonstrated that SpoIVB75-426-S378A adopts a monomeric form with a folded but flexible structure in solution, while the S378A mutation alters its hydrodynamic radius (RH) and overall compactness. These findings provide new insights into the structural dynamics of SpoIVB, including its monomeric state, PDZ domain interactions, and the functional implications of the S378A mutation. This study lays the groundwork for further investigations into the mechanistic role of SpoIVB in biological systems and its potential as a therapeutic target.IMPORTANCESporulation factor IV B protease (SpoIVB) is a pivotal PDZ-protease regulating the sigma K checkpoint during bacterial sporulation, yet its structural and mechanistic details remain elusive. This study provides the first atomic-resolution crystal structure of a SpoIVB variant (SpoIVB101-426-S378A), revealing a non-canonical catalytic triad (His236-Ala378-Thr393) and a unique PDZ domain insertion into the serine protease core. Biophysical analyses demonstrate that the S378A mutation enhances structural compactness and monomeric stability, while small-angle X-ray scattering confirms flexibility in the N-terminal region. These findings challenge traditional views of serine protease mechanisms and unveil novel regulatory interactions between PDZ and catalytic domains. The structural insights advance understanding of SpoIVB's role in sigma K activation and lay a foundation for targeting PDZ-protease interfaces in antibacterial strategies. This work bridges critical gaps in bacterial developmental biology and highlights SpoIVB as a potential therapeutic target.
Keyword ：
Bacillus subtilis Bacillus subtilis crystal structure crystal structure SAXS SAXS SpoIVB SpoIVB
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| GB/T 7714 | Zhu, Jian , Zhang, Xu , Zhang, Xinyun et al. Structural characterization and biophysical analysis of recombinant SpoIVB variants: insights into PDZ and serine protease domain interactions [J]. | MICROBIOLOGY SPECTRUM , 2025 . |
| MLA | Zhu, Jian et al. "Structural characterization and biophysical analysis of recombinant SpoIVB variants: insights into PDZ and serine protease domain interactions" . | MICROBIOLOGY SPECTRUM (2025) . |
| APA | Zhu, Jian , Zhang, Xu , Zhang, Xinyun , Sun, Gaohui , Xu, Peng , Yuan, Cai et al. Structural characterization and biophysical analysis of recombinant SpoIVB variants: insights into PDZ and serine protease domain interactions . | MICROBIOLOGY SPECTRUM , 2025 . |
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BACKGROUND:FXIa (coagulation factor XIa) is considered as a promising antithrombotic target with reduced hemorrhagic liabilities. The objective of this study was to identify a small-molecule inhibitor of FXIa as a potential low-hemorrhagic anticoagulant.METHODS:A high-throughput virtual screening was conducted using a drug repurposing library with the catalytic domain of FXIa as the bait. The identified inhibitor's anticoagulant activity was evaluated in vitro and in both arterial and venous murine thrombotic models. The dependency of the inhibitor on FXIa was further examined using FXI-/- mice. Hemorrhagic risks were subsequently evaluated in models of both localized and major bleeding.RESULTS:Virtual screening led to the identification of montelukast, a commonly used antiasthmatic drug, as a potent and specific FXIa inhibitor (half maximal inhibitory concentration of 0.17 mu mol/L). MK exhibited anticoagulant effects comparable to those of 2 mostly prescribed anticoagulants (warfarin and apixaban) in both arterial and venous thrombotic models. Notably, in stark contrast to the pronounced hemorrhagic risks of warfarin and apixaban, MK did not measurably increase the tendency of localized or major bleeding. Furthermore, MK did not prolong the time to arterial thrombotic occlusion in FXI-/- mice, while effectively inhibited arterial occlusion induced by the reinfusion of recombinant FXIa, confirming that MK's anticoagulant activity is mediated by plasma FXIa. Additionally, MK ameliorated inflammation levels and mitigated pulmonary microthrombus formation in a septic mouse model. Moreover, combination therapy with MK enhanced the antithrombotic effects of antiplatelets without an obvious increase of hemorrhage.CONCLUSIONS:This proof-of-concept study suggests the potent low-hemorrhage antithrombotic effect of MK by targeting FXIa and unveiling a new therapeutic application of MK.
Keyword ：
anticoagulants anticoagulants factor XI factor XI mice mice montelukast montelukast thrombosis thrombosis
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| GB/T 7714 | Zhou, Yang , Wang, Dong , Wu, Juhong et al. Discovery of the Low-Hemorrhagic Antithrombotic Effect of Montelukast by Targeting FXIa in Mice [J]. | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY , 2025 , 45 (4) : e150-e162 . |
| MLA | Zhou, Yang et al. "Discovery of the Low-Hemorrhagic Antithrombotic Effect of Montelukast by Targeting FXIa in Mice" . | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY 45 . 4 (2025) : e150-e162 . |
| APA | Zhou, Yang , Wang, Dong , Wu, Juhong , Qi, Yingying , Song, Meiru , Yao, Huiqiao et al. Discovery of the Low-Hemorrhagic Antithrombotic Effect of Montelukast by Targeting FXIa in Mice . | ARTERIOSCLEROSIS THROMBOSIS AND VASCULAR BIOLOGY , 2025 , 45 (4) , e150-e162 . |
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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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Antimicrobial peptides (AMPs) are powerful tools in combating drug-resistant bacteria. However, their clinical application is hindered by poor pharmacokinetics and suboptimal antimicrobial activity. This study proposes a strategy to enhance the antimicrobial activity and biosafety of AMPs by modification with albumin-binding molecules (ABMs). This strategy was validated by employing two model peptides with moderate antimicrobial efficacy. First, ABM modification stabilizes the secondary structures, facilitating bacterial membrane disruption. Additionally, modified AMPs target albumin in blood vessels, reducing renal clearance in vivo. Moreover, this binding minimizes contact with blood and endothelial cells, consequently diminishing vascular toxicity without compromising antimicrobial activity. Molecular dynamic simulations followed by experimental validation revealed new molecular insights into the mechanism underlying AMP-mediated membrane disruption, confirming our design strategy. This dual mechanism, structural stabilization and albumin-mediated pharmacokinetic enhancement, addresses the key limitation of AMPs, offering a versatile approach to develop potent, systemically safe antimicrobial therapies.
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| GB/T 7714 | Zhou, Yang , Wu, Juhong , Lin, Haili et al. Modifying Antimicrobial Peptides with Albumin-Binding Molecules Enhances Membrane-Disrupting Efficacy by Modulating the Secondary Structure [J]. | JOURNAL OF MEDICINAL CHEMISTRY , 2025 , 68 (12) : 12658-12674 . |
| MLA | Zhou, Yang et al. "Modifying Antimicrobial Peptides with Albumin-Binding Molecules Enhances Membrane-Disrupting Efficacy by Modulating the Secondary Structure" . | JOURNAL OF MEDICINAL CHEMISTRY 68 . 12 (2025) : 12658-12674 . |
| APA | Zhou, Yang , Wu, Juhong , Lin, Haili , Song, Meiru , Deng, Lina , Mai, Yuhan et al. Modifying Antimicrobial Peptides with Albumin-Binding Molecules Enhances Membrane-Disrupting Efficacy by Modulating the Secondary Structure . | JOURNAL OF MEDICINAL CHEMISTRY , 2025 , 68 (12) , 12658-12674 . |
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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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Phosphatidylserine is a crucial component of the cell membrane, typically localized to the inner leaflet of the lipid bilayer. In neoplastic cells, phosphatidylserine is aberrantly externalized, rendering it a promising biomarker for the development of targeted oncological therapeutics. We previously elucidated the crystal structure of phosphatidylserine bound to the C2 domain of lactadherin (LAC) and revealed calcium-independent binding with nanomolar affinity (Kd = 3.3 +/- 0.5 nM). Expanding upon our previous work, here we developed a novel targeted therapeutic platform by genetically fusing LAC with human serum albumin (HSA). This engineered LAC-HSA fusion protein synergistically integrates phosphatidylserine-targeting specificity with HSA's pharmacokinetic advantages, including an extended plasma half-life and drug delivery capabilities. To validate its therapeutic potential, we incorporated a potent cytotoxic agent (zinc monocarboxyphthalocyanine, CPZ) into LAC-HSA via a non-covalent strategy. In vitro, the LAC-HSA fusion protein selectively bound to phosphatidylserine-exposed tumor cells, enhancing the uptake of encoded cytotoxic agent (3-fold higher than the non-targeted control), thereby improving tumor cell-killing efficacy. In vivo, in the mouse solid tumor model, the targeted therapy group showed a 3-fold reduction in tumor volume compared to the non-targeted treatment group. These results clearly demonstrate that LAC-HSA is an effective phosphatidylserine-targeting drug carrier.
Keyword ：
Drug delivery Drug delivery Lactadherin Lactadherin Phosphatidylserine Phosphatidylserine
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| GB/T 7714 | Hu, Jing , Li, Lei , Wang, Tongyao et al. Engineering a phosphatidylserine-targeting drug carrier based on lactadherin C2 domain fused with human serum albumin for tumor therapy [J]. | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 319 . |
| MLA | Hu, Jing et al. "Engineering a phosphatidylserine-targeting drug carrier based on lactadherin C2 domain fused with human serum albumin for tumor therapy" . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 319 (2025) . |
| APA | Hu, Jing , Li, Lei , Wang, Tongyao , Wang, Zhiyou , Li, Jiahui , Xu, Peng et al. Engineering a phosphatidylserine-targeting drug carrier based on lactadherin C2 domain fused with human serum albumin for tumor therapy . | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES , 2025 , 319 . |
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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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