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学者姓名：黄明东
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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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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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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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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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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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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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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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