Bioconjugate Chemistry最新文献

{"title":"Reversible Protein Labeling via Genetically Encoded Dithiolane-Containing Amino Acid and Organoarsenic Probes.","authors":"Jiyeun Ahn, Taegwan Kim, Jieun Bae, Jinjoo Jung, Jeongeun Lee, Hwiyoung Lee, Jinhee Mun, Sohee Kim, Jongmin Park, Jonghoon Kim, Minseob Koh","doi":"10.1021/acs.bioconjchem.5c00078","DOIUrl":"10.1021/acs.bioconjchem.5c00078","url":null,"abstract":"<p><p>Conventional protein labeling techniques often rely on irreversible covalent bonds, limiting dynamic control over protein modifications. Here, we present a reversible protein labeling strategy using genetically encoded dithiolane-containing amino acid (dtF) and organoarsenic conjugation chemistry. Using dithiarsolane dicarboxylic acid probe A2, we achieved near-quantitative labeling and ethanedithiol-mediated removal within 1 h at room temperature. A2 exhibited reduced toxicity with a 7-fold higher IC₅₀ compared to arsenoxide, and its fluorescent derivative A2-FB showed no cytotoxicity up to 100 μM, enabling live-cell applications. This is the first demonstration of dithiol-arsenic chemistry at a single amino acid residue, providing a structural alternative to dicysteine motifs. Reversible labeling was validated in purified proteins (sfGFP-Y151dtF and MYO-K99dtF) and live <i>Escherichia coli</i>, offering a versatile tool for dynamic protein modifications and molecular tracking in biological systems.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1034-1039"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951234","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Positron Emission Tomography and Optical Imaging to Monitor Bioorthogonal Diels-Alder Click Chemistry of Trastuzumab with a Porphyrin.","authors":"Sara R D Gamelas, Shayla Shmuel, Cristina Simó, Alex Vanover, João P C Tomé, Augusto C Tomé, Leandro M O Lourenço, Patrícia M R Pereira","doi":"10.1021/acs.bioconjchem.5c00056","DOIUrl":"10.1021/acs.bioconjchem.5c00056","url":null,"abstract":"<p><p>Click chemistry to allow <i>in vivo</i> conjugation of a fluorophore porphyrin (Por)-tetrazine (Tz) with the human epidermal growth factor receptor 2 (HER2)-targeting trastuzumab conjugated with trans-cyclooctene (TCO) is described here. <i>In vitro</i> experiments confirmed successful click reactions between Por-Tz and trastuzumab-TCO and validated preserved trastuzumab immunoreactivity (no significant change in HER2 binding, <i>p</i> > 0.05). Positron emission tomography (PET) of [⁸⁹Zr]Zr-DFO-trastuzumab-TCO demonstrated 17.1 ± 2.9% injected dose per gram of tumor at 48 h postinjection. Optical imaging showed an ∼10-fold increase in the click group for Por-Tz when compared with Por-Tz alone. This preclinical data demonstrate a pretargeted approach for dual PET and optical imaging of HER2-expressing tumors.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1013-1020"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951372","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Gold Nanoparticles Coated with Nucleic Acids: An Overview of the Different Bioconjugation Pathways.","authors":"Raphaël Dutour, Gilles Bruylants","doi":"10.1021/acs.bioconjchem.5c00098","DOIUrl":"https://doi.org/10.1021/acs.bioconjchem.5c00098","url":null,"abstract":"<p><p>Gold-based nanomaterials have marked the last few decades with the emergence of new medical technologies presenting unique features. For instance, the conjugation of gold nanoparticles (AuNPs) and nucleic acids has allowed the creation of nanocarriers with immense promise for gene therapy applications. Although the use of lipid particles as RNA delivery vectors has been broadly explored, this review aims to focus on the limited models reported for the conjugation of RNA with AuNPs. This is nonetheless unexpected regarding the manifold strategies existing to conjugate DNA to gold nanoparticles, which are exhaustively listed in this paper. Furthermore, new processes such as fast microwave and freezing methods have been described very recently, and it therefore seemed necessary to review these recent but promising conjugation pathways and to pick out those applicable to RNA. Indeed, RNA is considerably more attractive than DNA for therapeutic purposes, but its low stability involves numerous difficulties in the construction of effective nanodevices. However, from the many approaches developed for DNA, it turns out that just two of them are frequently used for the building of RNA delivery platforms based on gold: the salt-aging method with thiolated RNA strands and physisorption. However, both approaches present strong limitations such as the low stability of the Au-S bond and the potential cytotoxicity of polycations. To conclude, this general assessment highlights that the exploration of innovating approaches implying different chemistries is needed for the creation of more robust and shapeable AuNPs-RNA conjugates.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":""},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144109058","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioorthogonally Activatable Photosensitizer for NIR Fluorescence Imaging-Guided Highly Selective Elimination of Senescent Tumor Cells and Chemotherapy Enhancement.","authors":"Yun Feng, Zifan Zhu, Shirui Zhao, Xingyu Jiang, Wen Zhang, Zhiai Xu","doi":"10.1021/acs.bioconjchem.5c00109","DOIUrl":"10.1021/acs.bioconjchem.5c00109","url":null,"abstract":"<p><p>Chemotherapy is a primary modality in cancer treatment, but it may induce cellular senescence, which in turn triggers the release of senescence-associated secretory phenotypes (SASPs) that promote tumor growth and metastasis. To selectively identify senescent cells and mitigate their negative impact on cancer therapy, herein, we have developed a β-galactosidase (β-Gal)-activated and self-immobilizing photosensitizer CyGF-DBCO-T. This photosensitizer can be selectively activated and fluorescently label proteins in situ within senescent cells, enabling near-infrared (NIR) fluorescence imaging-guided photodynamic therapy (PDT) for the precise ablation of these cells. First, we developed an activatable NIR fluorescent probe CyGF-N₃ that can specifically in situ label senescent cells. Subsequently, DBCO-T with free radicals underwent a bioorthogonal click reaction with activated CyGF-N₃ in senescent cells to generate the photosensitizer CyO-DBCO-T. Under light irradiation, CyO-DBCO-T generated singlet oxygen (¹O₂) in situ, thereby enabling precise PDT with fluorescence guidance and photoactivation. Both CyGF-N₃ and DBCO-T were encapsulated in biotinylated liposomes (CyGF-N₃@LIP-B and DBCO-T@LIP-B), which enhanced their water solubility, tumor targeting, and in vivo circulation time. This promoted the accumulation of the probes in senescent tumor cells, thus enabling intense fluorescence imaging of tumor senescence regions in mice and enhancing the efficacy of PDT. This dual-module strategy, guided by fluorescence imaging for PDT, has achieved selective identification and precise ablation of senescent tumor cells in a chemotherapy-induced senescence model, effectively alleviating chemotherapy resistance and suppressing tumor growth.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1066-1078"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143950737","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"GSH-Responsive Heterodimeric Dual-Targeted Nanomedicine Modulates EMT to Conquer Paclitaxel-Induced Invasive Breast Cancer Metastasis.","authors":"Ying Chen, Yao Chen, Hong Xu, Jianan Liu, Yan Wang, Yingjie Zeng, Hongyu Chen, Yuening Cao, Chen Sun, Xian Ge, Tingting Zhang, Xiaoke Shi, Xiujun Cao, Yilan Liu, Bo Ren, Tianbao Wang, Jun Lu","doi":"10.1021/acs.bioconjchem.5c00145","DOIUrl":"10.1021/acs.bioconjchem.5c00145","url":null,"abstract":"<p><p>Paclitaxel (PTX), although effective against primary breast cancer, presents formidable clinical challenges due to severe toxicity and pro-metastatic potential, a critical concern as distant metastasis causes 90% of breast cancer-related deaths. To address these limitations, we designed and prepared a tumor microenvironment-responsive nanoprodrug, PTX-SS-3'HPT@RGD-HA NPs, that engineered RGD peptide-modified hyaluronic acid (HA) nanocarriers encapsulating the antimetastatic 3'-hydroxy pterostilbene (3'HPT) and PTX heterodimer linked by a glutathione (GSH)-cleavable disulfide bond. These nanoparticles targeting CD44 and αvβ receptors overexpressed in aggressive breast cancer cells and synergized enhanced permeability and retention effects with receptor-mediated endocytosis, facilitating superior tumor-specific drug deposition and GSH-activated payload release <i>in vitro</i> and <i>in vivo</i>. Moreover, PTX-SS-3'HPT@RGD-HA NPs achieved excellent tumor growth inhibition while mitigating systemic toxicity and metastatic risks in 4T1 tumor-bearing mice. Mechanistically, 3'HPT counteracted PTX-induced epithelial-mesenchymal transition by downregulating MMP-9/N-cadherin and restoring E-cadherin expression, thereby neutralizing PTX-triggered pro-metastatic effects. This study pioneers a dual-targeted, toxicity-shielding nanoplatform that simultaneously improves therapeutic efficacy and addresses chemotherapy-driven metastasis, offering a revolutionary strategy for managing highly invasive breast cancer.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1098-1112"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951309","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tumor Cell Membrane Biomimetic Mesoporous Silicon Materials in Combination with PD-L1 Knockout Achieved through the CRISPR/Cas9 System for Targeted and Immunotherapeutic Purposes.","authors":"Jinjin Zhao, Xiaorou Wang, Haiguang Zhang, Qunmei Zhang, DeYing Bo, Hua Zhong, Luyang Jiao, Hongchang Yuan, Guangjian Lu","doi":"10.1021/acs.bioconjchem.5c00001","DOIUrl":"10.1021/acs.bioconjchem.5c00001","url":null,"abstract":"<p><p>Nanoparticle-based drug delivery systems, which enable the effective and targeted delivery of chemotherapeutic drugs to tumors, have revolutionized cancer therapy. Mesoporous silicon materials (MSN) have emerged as promising candidates for drug delivery due to their unique properties. The therapeutic efficacy can be significantly enhanced when treatments exhibit both targeting and antiphagocytic properties. In this study, cell membranes extracted from B16-F10 cells were used to encapsulate carboplatin (CBP)-loaded MSN via physical extrusion. Additionally, we intratumorally injected a plasmid containing the CRISPR/Cas9 system to achieve PD-L1 knockout, thereby reactivating the immune system. The cell membrane coating endowed the CBP@MSN with excellent slow-release capability and cytocompatibility. Enhanced tumor cell uptake of CBP@MSN@M was observed due to homologous targeting by cancer cell membranes. Moreover, CBP@MSN@M demonstrated enhanced antitumor efficacy in vivo and promoted the proliferation of immune cells. Finally, the antitumor effect was further improved by the knockout of PD-L1 within the tumor microenvironment. These results suggest that the newly prepared CBP@MSN@M, combined with PD-L1 knockout, holds significant potential as an effective therapeutic approach for treating tumors.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"971-979"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143952149","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Super-Sensitive Chemiluminescent Probe for the Detection of Caspase-3 Activity.","authors":"Rozan Tannous, Chi Zhang, Doron Shabat","doi":"10.1021/acs.bioconjchem.5c00151","DOIUrl":"10.1021/acs.bioconjchem.5c00151","url":null,"abstract":"<p><p>Caspase-3 is a pivotal enzyme in the apoptosis pathway that is responsible for executing programmed cell death through the cleavage of key cellular proteins. Existing fluorescence-based probes for caspase-3 detection suffer from limitations such as background noise from tissue autofluorescence and light scattering, reducing their sensitivity and real-time imaging capabilities. To overcome these limitations, we developed a chemiluminescent probe, Ac-DEVD-CL, that enables the highly sensitive and selective detection of caspase-3 activity. Upon caspase-3-mediated cleavage, the probe undergoes a self-immolative reaction that triggers a chemiluminescent signal, allowing real-time monitoring of the enzymatic activity. Probe Ac-DEVD-CL demonstrated an exceptionally high turn-on response, with a 5000-fold increase in the chemiluminescent signal upon enzymatic activation. The probe exhibited notable specificity for caspase-3, with minimal cross-reactivity toward other biologically relevant proteases and tumor-associated enzymes. Additionally, inhibition studies using the caspase-3 inhibitor confirmed that the probe's activation is exclusively mediated by caspase-3. A direct comparison with the commercially available fluorescent probe revealed that probe Ac-DEVD-CL offers significantly improved sensitivity, achieving a signal-to-noise ratio 380-fold higher and a limit of detection 100-fold lower. These results establish probe Ac-DEVD-CL as a highly effective tool for detecting caspase-3 activity with superior precision. Finally, we validated the probe's utility in imaging apoptosis in live cells. In 4T1 breast cancer cells treated with cisplatin, Ac-DEVD-CL generated a strong chemiluminescent signal, with a three-order-of-magnitude enhancement compared to untreated cells. Overall, the probe Ac-DEVD-CL demonstrates a significant improvement in detection sensitivity, providing a powerful and versatile chemiluminescent probe for real-time imaging of caspase-3 activity. Its exceptional sensitivity and selectivity could make it a valuable tool for cancer research, drug discovery, and therapeutic monitoring.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1113-1120"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12100654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143954395","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Redesigning Ibuprofen for Improved Oral Delivery and Reduced Side Effects.","authors":"Szilvia H Toth, Anca D Stoica, Cristian Sevcencu","doi":"10.1021/acs.bioconjchem.4c00558","DOIUrl":"10.1021/acs.bioconjchem.4c00558","url":null,"abstract":"<p><p>Ibuprofen (IBP) is one of the most widely used nonsteroidal anti-inflammatory drugs (NSAIDs). Being well-known for its efficacy, long history of use, and reduced adverse events compared to other NSAIDs, IBP is authorized as an analgesic and antipyretic drug. IBP's mechanism of action consists of inhibiting cyclooxygenases, which are crucial oxidoreductases in prostaglandin synthesis and generation of inflammation and pain. However, despite being effective and relatively safe, IBP can still induce a dose-dependent toxicity which manifests mainly in the gastrointestinal system as ulcerations and altered mucosal blood flow and cytotoxicity characterized by mitochondrial dysfunction and increased membrane permeability in enterocytes and hepatocytes. Therefore, ongoing research is performed to improve the IBP's activity and treatment outcome, and one way to achieve such improvements is through reducing IBP's toxicity by designing less harmful but still effective novel IBP conjugates. The aim of this review is to summarize the latest achievements with IBP conjugation techniques that created such valuable IBP formulations less toxic than but as effective as the parent drug.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"893-913"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143951032","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mannosamine-Modified Poly(lactic-<i>co</i>-glycolic acid)-Polyethylene Glycol Nanoparticles for the Targeted Delivery of Rifapentine and Isoniazid in Tuberculosis Therapy.","authors":"Cong Peng, Haopeng Luan, Qisong Shang, Wei Xiang, Parhat Yasin, Xinghua Song","doi":"10.1021/acs.bioconjchem.5c00062","DOIUrl":"10.1021/acs.bioconjchem.5c00062","url":null,"abstract":"<p><p>Tuberculosis, caused by <i>Mycobacterium tuberculosis</i>, is the leading cause of mortality attributed to a single infectious agent. Following macrophage invasion, M. tuberculosis uses various mechanisms to evade immune responses and to resist antituberculosis drugs. This study aimed to develop a targeted drug delivery system utilizing mannosamine (MAN)-modified nanoparticles (NPs) composed of poly(lactic-<i>co</i>-glycolic acid)-polyethylene glycol (PLGA-PEG), loaded with rifapentine and isoniazid, to enhance macrophage-directed therapy and enhance bacterial elimination. PLGA-PEG copolymer was modified with mannosamine through an amidation reaction. Rifapentine- and isoniazid-loaded PLGA-PEG-MAN NPs were synthesized by using the double emulsion solvent evaporation technique. The NPs exhibited an average particle size of 117.67 nm and displayed favorable physicochemical properties without evidence of cellular or hemolytic toxicity. The drug loading rates were 11.73% for rifapentine and 5.85% for isoniazid. Sustained drug release was achieved over a period exceeding 72 h, with antibacterial activity remaining intact during encapsulation. Synergistic bactericidal effects were noted. Additionally, mannosamine-modified NPs enhanced the phagocytic activity of macrophages via mannose receptor-mediated endocytosis, thereby improving drug delivery efficiency and significantly boosting the antibacterial efficacy of the NPs within macrophages. Pathological staining and biochemical analysis of rat organs following intravenous injection indicated that the NPs did not cause any significant toxic side effects in vivo. The findings of this study indicate that mannosamine-modified PLGA-PEG NPs loaded with rifapentine and isoniazid represent a promising drug delivery system for targeting macrophages to enhance the efficacy of antitubercular therapy.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"1021-1033"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12100642/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143955594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of a Long-Acting Myeloid-Derived Growth Factor via Site-Specific PEGylation.","authors":"Yong-Shan Zheng, Teng Zhang, Ji-Yang Song, Mingchan Liang, Ya-Li Liu, Zeng-Guang Xu, Cheng He, Zhan-Yun Guo","doi":"10.1021/acs.bioconjchem.5c00026","DOIUrl":"10.1021/acs.bioconjchem.5c00026","url":null,"abstract":"<p><p>Extracellular myeloid-derived growth factor (MYDGF) can improve organ repair. However, short <i>in vivo</i> half-life hampers its therapeutic application. Herein, we developed a long-acting MYDGF via site-specific PEGylation at its C-terminus. Bacterially overexpressed human MYDGF carrying a C-terminal Asn-Ala-Leu tripeptide motif was first ligated with a synthetic azido-functionalized Gly-Ile-Gly-Lys(N3) tetrapeptide linker via catalysis of [G238 V]BmAEP1, an engineered bamboo-derived asparaginyl endopeptidase (AEP)-type peptide ligase. Thereafter, the azido-functionalized MYDGF was efficiently conjugated with a commercially available dibenzocyclooctyne (DBCO)-functionalized linear PEG30000 via copper-free click chemistry. The site-specifically PEGylated MYDGF (PEG-MYDGF) retained high <i>in vitro</i> activity and showed a much longer <i>in vivo</i> half-life in mice compared with unmodified MYDGF. In diabetic mice, PEG-MYDGF significantly promoted wound healing after subcutaneous injection. Thus, PEG-MYDGF represents a long-acting biologic with therapeutic potential. The present enzymatic peptide ligation and copper-free click chemistry-based approach could be applied to other proteins for site-specific conjugation with various functional moieties.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"993-1003"},"PeriodicalIF":4.0,"publicationDate":"2025-05-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143954284","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}