Bioconjugate Chemistry最新文献

{"title":"Lysosome-Targeting Chimera Using Mannose-6-Phosphate Glycans Derived from Glyco-Engineered Yeast.","authors":"Seobin Kim, Jiyeon Kang, Danbi An, Jinho Seo, Doo-Byoung Oh","doi":"10.1021/acs.bioconjchem.4c00512","DOIUrl":"10.1021/acs.bioconjchem.4c00512","url":null,"abstract":"<p><p>Lysosome-targeting chimeras (LYTACs) harness the cell's lysosomal degradation machinery to break down extracellular and membrane proteins. Previous methods used a synthetic glycopeptide containing multiple serine-O-mannose-6-phosphate (poly-M6Pn), which presented challenges such as synthetic complexity and potential immunogenicity associated with poly-M6Pn. This study introduced a LYTAC formulation, LYTAC^gyM6pG, which uses glyco-engineered yeast-derived mannose-6-phosphate glycans (gyM6pGs) for lysosomal transport, overcoming synthetic complexities and immunogenic risks. The gyM6pGs used in LYTAC^gyM6pG are human-compatible (identical to the structures found in humans) and are efficiently produced through yeast fermentation, followed by the preparation of cell wall glycans and their <i>in vitro</i> modifications. We employed copper-free click chemistry (azide and dibenzocyclooctyne reactions) for the robust conjugation of gyM6pGs to a nanobody targeting the immune checkpoint protein PD-L1, thereby streamlining the assembly of LYTAC^gyM6pG. We demonstrated that LYTAC^gyM6pG effectively degraded endogenous and recombinant PD-L1 proteins on the cell surface by directing them to the lysosome via the cation-independent mannose-6-phosphate receptor pathway. Furthermore, LYTAC^gyM6pG significantly enhanced T cell-mediated cytotoxicity against cancer cells, surpassing the efficacy of nanobodies alone. The successful application of gyM6pGs in the development of LYTAC^gyM6pG highlights the potential for a more viable and scalable therapeutic production of LYTACs, paving the way for broader therapeutic applications, including cancer treatment.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"424-436"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143530904","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":"Selenalysine as a Chemical Tool for Probing Histone Post-Translational Modifications.","authors":"Sandra Pinzón Martín, Jasmin Mecinović","doi":"10.1021/acs.bioconjchem.4c00567","DOIUrl":"10.1021/acs.bioconjchem.4c00567","url":null,"abstract":"<p><p>Post-translational modifications (PTMs) on histones play a crucial role in determining the structure and function of chromatin, thereby regulating the eukaryotic gene expression. Histone lysine methylation and acetylation are among the most widespread and biomedically important PTMs, with new chemical tools for their examination in high demand. Here, we report the first use of γ-selenalysine as an efficient lysine mimic for enzymatic methylation, acetylation, and deacetylation reactions catalyzed by histone lysine methyltransferases, acetyltransferases, and a deacetylase. We also show that easily accessible selenocysteine and cysteine residues can undergo chemo- and site-selective alkylation reactions to generate both unmodified and modified γ-selenalysine and related γ-thialysine residues in histone peptides. This dual-modification strategy enables the site-specific incorporation of two distinct functionalities into peptides, mimicking lysine post-translational modifications commonly found on histones. Our research presents a novel approach in which selenocysteine serves as a unique handle for the chemoselective introduction of selenalysine, along with its methylated and acetylated analogues. These tools are designed to facilitate the study of epigenetic proteins that are important for human health and disease.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"510-520"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143555306","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":"Scalable One-Pot Production of Geranylgeranylated Proteins in Engineered Prokaryotes.","authors":"Md Shahadat Hossain, Md Mahbubul Alam, Zhiwei Huang, Faeze Mousazadeh, Ronit Sarangi, Ebbing de Jong, Kavindu C Kolamunna, Albert L Adhya, James L Hougland, Atanu Acharya, Davoud Mozhdehi","doi":"10.1021/acs.bioconjchem.4c00493","DOIUrl":"10.1021/acs.bioconjchem.4c00493","url":null,"abstract":"<p><p>Geranylgeranylation is a critical post-translational modification essential for various cellular functions. However, current methods for synthesizing geranylgeranylated proteins are complex and costly, which hinders access to these proteins for both biophysical and biomaterials applications. Here, we present a method for the one-pot production of geranylgeranylated proteins in <i>Escherichia coli</i>. We engineered <i>E. coli</i> to express geranylgeranyl pyrophosphate synthase (GGS), an enzyme that catalyzes the production of geranylgeranyl pyrophosphate. By coexpressing GGS with a geranylgeranyltransferase, we achieved efficient geranylgeranylation of model protein substrates, including intrinsically disordered elastin-like polypeptides (ELPs) and globular proteins such as mCherry and the small GTPases RhoA and Rap1B. We examined the biophysical behavior of the resulting geranylgeranylated proteins and observed that this modification affects the phase-separation and nanoassembly of ELPs and lipid bilayer engagement of mCherry. Taken together, our method offers a scalable, versatile, and cost-effective strategy for producing geranylgeranylated proteins, paving the way for advances in biochemical research, therapeutic development, and biomaterial engineering.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"415-423"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11926785/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143539491","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":"Unlocking the Potential of Antimicrobial Peptides: Cutting-Edge Advances and Therapeutic Potential in Combating Bacterial Keratitis.","authors":"Bingru Xiao, Jie Wang, Jie Xing, Lulu He, Chen Xu, Aiguo Wu, Juan Li","doi":"10.1021/acs.bioconjchem.4c00594","DOIUrl":"10.1021/acs.bioconjchem.4c00594","url":null,"abstract":"<p><p>Bacterial keratitis is a prevalent, and severe corneal illness resulting from bacterial pathogens. Failure to administer a timely and suitable therapy may lead to corneal opacity, ulceration, significant vision impairment, or potential blindness. Current clinical interventions for bacterial keratitis involve the administration of topical antimicrobial agents and systemic antibiotics. However, the misuse and overuse of antibiotics have led to the rapid emergence of antibiotic-resistant bacteria. Additionally, the restricted antibacterial spectrum and possible adverse effects of antibiotics have provided considerable obstacles to traditional therapies. This highlights the urgent need for novel and highly effective antimicrobial agents. Antimicrobial peptides (AMPs) are a class of naturally occurring or synthetically designed small molecules that have gained significant attention due to their unique antimicrobial mechanisms and low risk of resistance development. AMPs exhibit promising potential in treating bacterial keratitis through direct antibacterial mechanisms, such as inhibiting cell wall synthesis, disrupting cell membranes, and interfering with nucleic acid metabolism, as well as indirect mechanisms, including modulation of the host immune response. This review provides a comprehensive overview of the antibacterial mechanisms of AMPs and their advancements in the treatment of bacterial keratitis. It emphasizes the role of various modification strategies and artificial-intelligence-assisted design in enhancing the antibacterial efficacy, stability, and biocompatibility of AMPs. Furthermore, this review discusses the latest progress in combining AMPs with delivery systems for improved therapeutic outcomes. Finally, the review highlights the current challenges and future perspectives of AMPs in bacterial keratitis treatment, providing valuable insights for developing novel AMPs with high antibacterial efficacy, stability, and safety for bacterial keratitis therapies.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"311-331"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143456265","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":"T Cell-Targeting Nanotherapies for Atherosclerosis.","authors":"Karla Lambaren, Noah Trac, Daniel Fehrenbach, Meena Madhur, Eun Ji Chung","doi":"10.1021/acs.bioconjchem.4c00590","DOIUrl":"10.1021/acs.bioconjchem.4c00590","url":null,"abstract":"<p><p>Cardiovascular diseases remain the leading cause of mortality worldwide. Specifically, atherosclerosis is a primary cause of acute cardiac events. However, current therapies mainly focus on lipid-lowering versus addressing the underlying inflammatory response that leads to its development and progression. Nanoparticle-mediated drug delivery offers a promising approach for targeting and regulating these inflammatory responses. In atherosclerotic lesions, inflammatory cascades result in increased T helper (Th) 1 and Th17 activity and reduced T regulatory activation. The regulation of T cell responses is critical in preventing the inflammatory imbalance in atherosclerosis, making them a key therapeutic target for nanotherapy to achieve precise atherosclerosis treatment. By functionalizing nanoparticles with targeting modalities, therapeutic agents can be delivered specifically to immune cells in atherosclerotic lesions. In this Review, we outline the role of T cells in atherosclerosis, examine current nanotherapeutic strategies for targeting T cells and modulating their differentiation, and provide perspectives for the development of nanoparticles specifically tailored to target T cells for the treatment of atherosclerosis.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"332-346"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143466434","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":"Hafnium-Doped Prussian Blue Nanoparticles with Homologous Tumor Targeting and Magnetic Resonance Imaging Ability for Enhanced Tumor Radiotherapy via Photothermal Therapy and Hypoxia Relief.","authors":"Ye Kuang, Yufang Chen, Xinying Liu, Baohui Liu, Yu Duan, Chaowei Hong, Jincong Yan, Renpin Liu, Yubin Zhuang, Changmai Chen, Wei Chen","doi":"10.1021/acs.bioconjchem.5c00064","DOIUrl":"10.1021/acs.bioconjchem.5c00064","url":null,"abstract":"<p><p>Radiotherapy (RT) continues to encounter significant obstacles such as formidable resistance, potential harm to adjacent healthy cells, and restricted effectiveness against tumors, resulting in a notable recurrence rate. Therefore, combining imaging, other treatments, and suitable enzyme activity in one nanoplatform can enhance the RT effect and reduce the damage to normal tissue. In this study, integrating hafnium in Prussian blue (PB) nanoparticles (PB NPs) provided innovative hafnium-doped PB (HPB) NPs as multifunctional radiosensitizers. The HPB NPs were enveloped by the cancer cell membrane, resulting in cancer cell membrane-camouflaged HPB (CMHPB) NPs that can specifically target homologous tumors. Moreover, owing to the inherent ability of photothermal therapy (PTT), magnetic resonance imaging (MRI), and catalase (CAT)-like activity of PB NPs, CMHPB NPs effectively overcome tumor hypoxia and realize the MRI-guided combined RT and PTT. The prepared HPB NPs possessed uniform and cubic morphology with a monodisperse size of approximately 80 nm and <i>T</i>₁ MRI capability (<i>r</i>₁ = 0.9309 mM^-1 S^-1). The HPB NPs showed reliable PTT efficiency and CAT-like activity in vitro and in vivo. Guided by MRI, the CMHPB NPs can be precisely delivered to the tumor region for combined RT and PTT for targeted destruction of tumor cells, significantly inhibiting tumor growth. The innovative multifunctional CMHPB NPs can be used for MRI-guided RT and PTT, which address the key challenges of RT and provide a viable strategy for enhancing tumor treatment.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"597-608"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143575560","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":"Targeted Delivery of TLR7 Agonists to the Tumor Microenvironment Enhances Tumor Immunity via Activation of Tumor-Resident Myeloid Cells.","authors":"Emanuela Sega, Srikanth Kotapati, Yam B Poudel, Qinqin Cheng, Keerthi Sadanala, Bridget Schneider, Eugene P Chekler, Chetana Rao, Sanjeev Gangwar, Tim Sproul, Deborah Law, Miranda Broz, Pavel Strop, Sayumi Yamazoe","doi":"10.1021/acs.bioconjchem.4c00534","DOIUrl":"10.1021/acs.bioconjchem.4c00534","url":null,"abstract":"<p><p>Toll-like receptors (TLR) are phylogenetically conserved mediators of innate immunity that are essential for establishing adaptive immune responses against invading pathogens. TLR7 is an endosomal receptor expressed predominantly in myeloid and B cells. Activation of TLR7 induces Type I interferon and proinflammatory responses; therefore, targeting TLR7 is a promising strategy for antitumor therapy. Although the use of bacterial components to trigger innate immune responses in cancer patients started a century ago, the effectiveness of systemic TLR agonists has been rather underwhelming in clinical trials, partly due to nonspecific immune activation leading to safety and tolerability issues. Antibody-drug conjugates (ADCs) constitute a proven therapeutic modality amenable to systemic administration with limited toxicity concerns via a targeted delivery platform. We generated TLR7 agonist-antibody conjugates that recognize tumor antigens expressed on the surface of tumor cells. Generated ADCs demonstrated robust activity in in vitro tumor antigen-presenting cell (APC) coculture systems as indicated by dose-dependent upregulation of PD-L1 and CD86 on macrophages. TLR7 agonist-ADC provided superior tumor growth control compared to intravenously (IV) administrated free TLR7 agonist. Treatment with TLR7 agonist-ADC led to prolonged activation of myeloid cells in the tumor microenvironment (TME) with minimum immune activation in the periphery. Systemic and tissue exposure studies demonstrated tumor-specific free drug release by targeted ADC treatment. In summary, the TLR7 agonist-ADC can potentially activate immune cells in the TME to generate tumor antigen-specific T-cell responses, making it an attractive approach for precision cancer therapy.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"437-448"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11926791/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143412270","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":"Conditional Control of Benzylguanine Reaction with the Self-Labeling SNAP-tag Protein.","authors":"Steven E Caldwell, Isabella R Demyan, Gianna N Falcone, Avani Parikh, Jason Lohmueller, Alexander Deiters","doi":"10.1021/acs.bioconjchem.5c00002","DOIUrl":"10.1021/acs.bioconjchem.5c00002","url":null,"abstract":"<p><p>SNAP-tag, a mutant of the O⁶-alkylguanine-DNA-alkyltransferase, self-labels by reacting with benzylguanine (BG) substrates, thereby forming a thioether bond. SNAP-tag has been genetically fused to a wide range of proteins of interest in order to covalently modify them. In the context of both diagnostic and therapeutic applications, as well as use as a biological recording device, precise control in a spatial and temporal fashion over the covalent bond-forming reaction is desired to direct inputs, readouts, or therapeutic actions to specific locations, at specific time points, in cells and organisms. Here, we introduce a comprehensive suite of six caged BG molecules: one light-triggered and five others that can be activated through various chemical and biochemical stimuli, such as small molecules, transition metal catalysts, reactive oxygen species, and enzymes. These molecules are unable to react with SNAP-tag until the trigger is present, which leads to near complete SNAP-tag conjugation, as illustrated both in biochemical assays and on human cell surfaces. This approach holds promise for targeted therapeutic assembly at disease sites, offering the potential to reduce off-target effects and toxicity through precise trigger titration.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"540-548"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11926790/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143466431","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":"Effect of Lipidation on the Structure, Oligomerization, and Aggregation of Glucagon-like Peptide 1.","authors":"Eva Přáda Brichtová, Irina A Edu, Xinyang Li, Frederik Becher, Ana L Gomes Dos Santos, Sophie E Jackson","doi":"10.1021/acs.bioconjchem.4c00484","DOIUrl":"10.1021/acs.bioconjchem.4c00484","url":null,"abstract":"<p><p>Lipidated analogues of glucagon-like peptide 1 (GLP-1) have gained enormous attention as long-acting peptide therapeutics for type 2 diabetes and also antiobesity treatment. Commercially available therapeutic lipidated GLP-1 analogues, semaglutide and liraglutide, have the great advantage of prolonged half-lives <i>in vivo</i> of hours and days instead of minutes as is the case for native GLP-1. A crucial factor in the development of novel lipidated therapeutic peptides is their physical stability, which greatly influences manufacturing and drug product development. This work provides a systematic study of the solubility, structure, oligomerization, and long-term stability of five different lipidated analogues of GLP-1, varying in the position of the lipidation site and the nature of lipid attachment. The lipidation was found to negatively impact the peptide solubility, in all cases, limiting it to a specific pH range. An increase in the α-helical secondary structure was observed upon lipidation, and the lipidated analogues were found to form larger and more stable oligomeric species compared to nonlipidated GLP-1. Importantly, the distributions and populations of oligomeric species formed were regulated by both the position and the nature of the lipidation. During the 6 days of sample aging, several lipidated analogues formed aggregates with variable morphologies ranging from elongated mature fibrils to amorphous structures. The kinetics of aggregation often showed multiple steps and did not follow a standard nucleation-propagation mechanism. A wide range of behaviors was observed, and while our observations indicate that the formation of a single stable oligomer results in the greatest physical stability, positioning the lipid group toward the N-terminus of the peptide results in extremely rapid amyloid formation. We believe that our study provides important findings for the development of long-acting lipidated analogues of peptide therapeutics.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"401-414"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11926786/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142996179","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":"Chemical Synthesis and Poly(ethylene glycol)-Like Conjugation of the Mango-II Fluorogenic RNA Aptamer.","authors":"Maria Nerantzaki, Claire Husser, Isaure Sergent, Laurence Charles, Jean-François Lutz, Michael Ryckelynck","doi":"10.1021/acs.bioconjchem.4c00540","DOIUrl":"10.1021/acs.bioconjchem.4c00540","url":null,"abstract":"<p><p>A reliable method for the efficient chemical synthesis and poly(ethylene glycol) PEG-like modification of fluorogenic RNA aptamers is reported. The 43-mer version of Mango-II RNA (MangoII-v1), which binds tightly and specifically to the green fluorophore TO1-Biotin (TO1-B), was synthesized by automated phosphoramidite chemistry using 2'-<i>O</i>-[(triisopropylsilyl)oxy]methyl] (2'-<i>O</i>-TOM)-protected ribonucleosides. Solid-phase phosphoramidite chemistry was also used as a single tool to prepare MangoII-v1 modified with a PEG-like oligophosphate synthetic segment (MangoII-v1-<b>P</b>). After cleavage from the resin, deprotection, and purification, the capacity to activate the fluorescence of TO1-B and the degradation behavior of the chemically synthesized RNAs MangoII-v1 and MangoII-v1-<b>P</b>, were deeply investigated in comparison with those of the enzymatically synthesized 48 nucleotides long RNA MangoII. Interestingly, the chemically synthesized MangoII-v1 RNA aptamer demonstrated great activity toward its target, compared to the enzymatically synthesized analogue. Moreover, it was found to be highly stable, retaining its structural integrity and bioactivity, even after seven days of incubation in 20% fetal bovine serum. MangoII-v1-<b>P</b> also showed a high affinity for TO1-B and excellent degradation resistance.</p>","PeriodicalId":29,"journal":{"name":"Bioconjugate Chemistry","volume":" ","pages":"449-456"},"PeriodicalIF":4.0,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143466422","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}