RSC Chemical Biology最新文献

{"title":"Discovery of PROTACs recruiting the E3 ligase CHIP.","authors":"Tokiha Masuda-Ozawa, Shusuke Tomoshige, Eisuke Hayakawa, Shinichi Sato, Kenji Ohgane, Fumiaki Ohtake, Minoru Ishikawa","doi":"10.1039/d6cb00124f","DOIUrl":"10.1039/d6cb00124f","url":null,"abstract":"<p><p>Proteolysis-targeting chimeras (PROTACs) are promising degraders in targeted protein degradation (TPD) systems. Although more than 600 E3 ubiquitin (Ub) ligases exist in the human genome, only a few E3 ligases have been engaged in PROTACs. It is essential to expand the range of available E3 ligase resources to combat drug resistance caused by their mutations and to find suitable candidates for the degradation of certain target proteins. In this study, we aimed to develop novel PROTACs utilizing the carboxyl terminus of the Hsc70-interacting protein (CHIP) E3 ligase, which was previously unutilized. We designed and synthesized PROTACs conjugated with CHIP ligands and target protein ligands <i>via</i> linkers. These PROTACs form a ternary complex with CHIP and a target protein and ubiquitylate the target protein <i>in vitro</i>. Furthermore, taking advantage of the fact that CHIP is not an intricate multi-subunit E3 ligase, unlike other E3 ligases utilized for PROTACs, an <i>in vitro</i> ubiquitylation assay revealed that CHIP induced not only the lysine (K) 48-linked polyubiquitin (poly-Ub) chain, which is a typical proteasome degradation signal, but also the K63 linkage. Furthermore, it induces the proteasome-dependent degradation of HaloTag protein and endogenous bromodomain-containing protein 4 (BRD4). Thus, we successfully expanded the E3 ligase toolbox for PROTACs. These new PROTACs using CHIP, which induce non-canonical proteasome degradation signals containing a mixed linkage of poly-Ub chains on the target protein, can be applied to the degradation of other proteins, especially disease-related proteins.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":"1997-2013"},"PeriodicalIF":3.9,"publicationDate":"2026-09-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13592199/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149018120","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Semi-synthesis of the C-terminal region of <i>Pf</i>RALP1: an alternative strategy for producing a hard-to-express merozoite protein.","authors":"Akash Narayan, Sreejith Raran-Kurussi, Mrinal K Bhattacharyya, Kalyaneswar Mandal","doi":"10.1039/d6cb00176a","DOIUrl":"10.1039/d6cb00176a","url":null,"abstract":"<p><p><i>Plasmodium falciparum</i> rhoptry-associated leucine zipper-like protein 1 (<i>Pf</i>RALP1) is an indispensable protein involved in merozoite invasion of human red blood cells (RBCs), leading to the deadly malaria disease. <i>Pf</i>RALP1 is stored in the rhoptry neck of merozoites and translocated to the moving junction during invasion and is therefore regarded as a moving junction protein. The C-terminal region of the full-length <i>Pf</i>RALP1 (<i>Pf</i>RALP1-C1) plays a crucial role in binding to an unidentified receptor protein on erythrocytes during merozoite invasion. <i>Pf</i>RALP1 also elicits immunogenicity in <i>P. falciparum</i>-infected asymptomatic and semi-immune adults. Successful recombinant expression of <i>Pf</i>RALP1-C1 was demonstrated using a wheat germ cell-free extract system. However, obtaining pure recombinant <i>Pf</i>RALP1 in other heterologous systems has not yet been explored. We faced significant challenges in obtaining <i>Pf</i>RALP1-C1 in pure form in reasonable quantities through overexpression in <i>E. coli</i>. To address this issue, we introduce a semi-synthetic approach to obtain functional <i>Pf</i>RALP1-C1. Our findings include an efficient three-segment native chemical ligation of two chemically synthesized peptide segments and a recombinantly expressed polypeptide. The circular dichroism data for the semi-synthetic protein are consistent with the predicted secondary structure, which consists of intrinsically disordered regions and alpha helices. The semi-synthetic <i>Pf</i>RALP1-C1 retains the binding epitope and interacts with the unknown RBC receptor, as it competitively inhibits the invasion of RBCs by merozoites. Thus the semi-synthetic method described here offers a promising strategy for producing this difficult-to-express antigenic protein <i>Pf</i>RALP1-C1, with potential for large-scale production and downstream biological and therapeutic applications.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13617758/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149075927","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Conformational reprogramming of c-Myc <i>via</i> intracellular cyclisation.","authors":"Rachel A Johnson, Jody M Mason","doi":"10.1039/d6cb00191b","DOIUrl":"10.1039/d6cb00191b","url":null,"abstract":"<p><p>Intrinsically disordered transcription factors represent a major challenge for chemical biology. Their lack of persistent structure limits both functional interrogation and ligand discovery. Here, we show that intracellular covalent cyclisation can conformationally reprogram the intrinsically disordered c-Myc bHLHZip region into a more ordered, DNA-binding state independent of its obligate partner Max. Using cell-penetrating bis-alkylating crosslinkers and rationally positioned cysteine pairs, we introduced helix-stabilising constraints into c-Myc during intracellular recombinant expression in <i>E. coli</i>. Among multiple designs, a single constraint positioned within helix two uniquely induced helicity and increased thermal stability, enabling sequence-specific E-box binding in the absence of Max. Notably, this gain of function does not recapitulate the canonical Myc-Max coiled coil architecture, revealing that non-native but functional conformational states can support sequence-specific DNA recognition. These findings demonstrate that intracellular chemical constraint can provide access to structured states that are normally inaccessible in the unbound protein and obscured within native protein complexes. By decoupling conformational ordering from partner occupancy, this approach establishes conformational reprogramming as a strategy to render otherwise intractable proteins amenable to functional interrogation and ligand discovery.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":"1991-1996"},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13576623/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148978322","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting virus-glycan recognition in influenza viruses and coronaviruses: from the molecular principles to glycomimetic antivirals strategies.","authors":"Cristina Fernández-Pérez, María Emilia Cuervo, Iris A Bermejo, Jon Imanol Quintana, Ana Gimeno, Ana Ardá, Jesús Jiménez-Barbero, Luca Unione","doi":"10.1039/d6cb00215c","DOIUrl":"10.1039/d6cb00215c","url":null,"abstract":"<p><p>Glycans constitute the first molecular landscape encountered by viruses during infection and play fundamental roles in viral attachment, host adaptation, tissue tropism, and immune evasion. Far from being passive components of the cell surface, host glycans actively regulate virus-host interactions by functioning as attachment factors, entry receptors, or modulators of receptor engagement, while viral glycans contribute to immune escape and infectivity. Consequently, the molecular recognition of glycans has emerged as a major determinant of viral evolution and pathogenicity. This review presents our perspective on the structural and mechanistic principles that govern virus-glycan recognition, focusing on influenza viruses and coronaviruses as paradigmatic examples. We discuss how subtle variations in glycan structure, including glycosidic linkage, chain length, multivalent presentation, and chemical modifications such as <i>O</i>-acetylation, shape viral receptor specificity, host range, and cross-species transmission. Recent advances from structural biology, NMR spectroscopy, glycan arrays, computational modeling, and glycochemistry have substantially expanded our understanding of these dynamic recognition events and their evolutionary consequences. We further highlight how these insights are driving the development of glycomimetic antivirals designed to interfere with the earliest stages of infection. Approaches based on multivalent sialoglycan analogues, stabilized carbohydrate mimetics, and heparan sulfate-inspired scaffolds illustrate the growing potential of targeting glycan-mediated recognition as an alternative or complementary antiviral strategy. By integrating molecular recognition, viral adaptation, and medicinal chemistry, this review underscores the opportunities offered by glycobiology to develop innovative, potentially broad-spectrum antiviral therapeutics.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13613654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149065199","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Pt(iv) scaffold effects on nucleolar stress and DNA damage response pathways.","authors":"Christopher R Griffin, Victoria J DeRose","doi":"10.1039/d6cb00235h","DOIUrl":"10.1039/d6cb00235h","url":null,"abstract":"<p><p>The platinum compounds cisplatin and oxaliplatin are widely used anticancer agents. Although platinum compounds have long been thought to induce cell death through the DNA damage response (DDR), subsequent work has shown that oxaliplatin instead engages a nucleolar stress pathway characterized by disruptions to ribosome biogenesis. Importantly, tuning platinum compounds' non-labile ligand identity, particularly incorporation of the diaminocyclohexane (DACH) ligand, influences nucleolar stress induction. While effective, Pt(ii) drugs are limited by severe side effects arising, in part, from multiple targets as well as a lack of selectivity between malignant and non-malignant cells. The axial ligands of Pt(iv) compounds afford tunable properties that may improve selectivity. Here, we investigate how platinum compound ligand identity and oxidation state together dictate engagement of either the DDR or nucleolar stress pathway. Using a series of dicarboxylate Pt(iv) complexes derived from cisplatin and DACH-Pt scaffolds, we find that Pt(iv) compounds bearing aliphatic dicarboxylate axial ligands preserve the pathway specificity encoded by their Pt(ii) cores: cisplatin analogs primarily activate the DDR, whereas DACH-Pt analogs preferentially induce nucleolar stress. Increasing compound lipophilicity enhances antiproliferative activity and cellular accumulation, and accelerates pathway activation. However, analysis of uptake, response onset, and IC₅₀ values reveals that lipophilicity alone does not fully account for biological activity. Notably, we identify the most potent nucleolar stress inducer reported, a Pt(iv) compound requiring ∼1000-fold lower concentrations to trigger nucleolar stress than the DACH-Pt(ii) analogue. Together, these findings establish Pt(iv) ligand design as a strategy to optimize antiproliferative activity while selectively intensifying DDR or nucleolar stress.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13588258/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149009183","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.","authors":"Xuxue Liu, Xiangyang Gao, Sasipa Booranamonthol, Peng Wu, Rung-Yi Lai, Qi Zhang","doi":"10.1039/d6cb00249h","DOIUrl":"10.1039/d6cb00249h","url":null,"abstract":"<p><p>Radical <i>S</i>-adenosylmethionine (rSAM) enzymes constitute one of the largest and most versatile enzyme superfamilies in biology, catalyzing diverse radical-mediated reactions essential for metabolism, cofactor biosynthesis, nucleic acid modification, and natural product formation. Central to their chemistry is the reductive cleavage of <i>S</i>-adenosylmethionine (SAM) by an iron-sulfur cluster, generating the highly reactive 5'-deoxyadenosyl radical (5'-dAdo˙), which initiates a broad range of challenging transformations. Recent advances have expanded the reactivity of rSAM enzymes beyond their natural roles, revealing unprecedented mechanistic flexibility and synthetic potential. Photochemical activation strategies now enable light-driven reduction of [4Fe-4S] clusters in the presence of biological or chemical photosensitizers, thereby initiating radical formation. In parallel, cobalamin-dependent radical SAM methyltransferases have opened new avenues for ethyl and fluoromethyl transfer chemistry using corresponding SAM analogues. Notably, the use of a strategically engineered, stable analogue, such as 7-deazaadenine-tetrazole-substituted F-SAM (F-7dz-tSAM), has successfully overcome inherent cofactor degradation. Noncanonical radical reactivity, exemplified by ArsL-catalyzed C-As bond formation and NosL-mediated photoinduced trifluoromethylation, demonstrates the capacity of rSAM enzymes to perform new-to-nature transformations. Lastly, the repurposing of rSAM enzymes for formylglycine generation has enabled orthogonal aldehyde-tag formation for bioorthogonal protein labeling, further expanding their utility in chemical biology. Collectively, these advances establish rSAM enzymes as versatile platforms for radical biocatalysis, chemical biology, and new-to-nature chemistry.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13598754/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149041135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Affinity selection mass spectrometry screening discovers new COP1 peptide binders.","authors":"Harsha Negi, Noor Radhi, Nicolas Schiff, Sam A Jamieson, Deanna Shea, Martin Middleditch, Robert Mullin, Renata Kowalczyk, Paul W Harris, Peter D Mace, Daniel Conole","doi":"10.1039/d6cb00250a","DOIUrl":"10.1039/d6cb00250a","url":null,"abstract":"<p><p>Targeting E3 ubiquitin ligases with chemical probes remains a major challenge, despite their central roles in cellular regulation and disease. Constitutive photomorphogenic 1 (COP1) is an E3 ligase whose complex, adaptor-dependent biology has made its selective targeting difficult. Here, we develop a peptide-based affinity selection mass spectrometry (Pep-AS-MS) platform to discover new peptide based COP1 binders. Leveraging a mass spectrometry compatible library design, fluorescence-guided selection optimisation, and an open-source software driven target-decoy database strategy for peptide identification and quantification, we enable hit ranking from highly complex combinatorial libraries. Using this approach, we identify and validate six previously unreported COP1-binding peptides, including ligands with binding potencies comparable to the native TRIB1 motif. This work establishes a quantitative and accessible Pep-AS-MS framework for ligand discovery against challenging protein-protein interaction targets and provides new chemical tools to interrogate COP1 biology.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13586983/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149009148","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"One-pot enzymatic synthesis of the sugar nucleotide CDP-ribitol.","authors":"Saeed Akkad, Eva W Wan, Alex Maddison, Jessica Rule Mcloughlin, Cindy Au-Yeung, Lloyd D Murphy, Greg L McNeil, Lianne I Willems","doi":"10.1039/d6cb00172f","DOIUrl":"10.1039/d6cb00172f","url":null,"abstract":"<p><p>CDP-ribitol serves as an essential donor for d-ribitol-5-phosphate incorporation into bacterial and mammalian glycoconjugates. Here, we demonstrate the one-pot enzymatic synthesis of CDP-ribitol from the readily available precursor ribitol. We also explore the synthesis of bioorthogonally tagged derivatives and other CDP conjugates, thereby providing valuable new tools for glycoscience research.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":"1972-1977"},"PeriodicalIF":3.9,"publicationDate":"2026-09-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13576159/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148978282","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A truncated nisin variant, lipidated at its C-terminus, displays improved stability and increased antibacterial activity against methicillin-resistant <i>Staphylococcus aureus</i>.","authors":"Longcheng Guo, Chenhui Wang, Oscar P Kuipers, Jaap Broos","doi":"10.1039/d6cb00193a","DOIUrl":"10.1039/d6cb00193a","url":null,"abstract":"<p><p>The rise of bacterial resistance has prompted researchers to shift their focus toward alternative antimicrobial agents, including antimicrobial peptides (AMPs). Some naturally occurring AMPs are lipidated, showing similarity with clinically used antimicrobial agents such as daptomycin and polymyxins, which are lipidated peptides. In this study, we investigate the impact of various lipid modifications on nisin. Nisin is a well-studied 34-amino acid AMP, ribosomally synthesized and post-translational modified, which is effective against many Gram-positive bacteria and is widely used as a food preservative. Wild-type nisin and two truncated forms, nisin(1-31) and nisin(1-20) were conjugated at the C-terminus with either a C4, C6, C8, or C10 lipid tail. Antimicrobial activity was assessed against two Gram-positive strains: methicillin-resistant <i>Staphylococcus aureus</i> (MRSA) and vancomycin-resistant <i>Enterococcus faecium</i> (VRE). Our results show that the lipidation of wild-type nisin and nisin(1-31) reduced its antibacterial activity, with the longest chains exhibiting the lowest inhibitory effects. However, lipidation of the nisin fragment nisin(1-20), especially with C8 resulting in compound 12, enhanced its antibacterial activity and specificity against <i>S. aureus</i> species, making it four times more potent than wild-type nisin. Mode-of-action studies revealed that the lipidated construct 12 retained its ability to bind lipid II but does not induce pore formation in <i>S. aureus</i>. Notably, due to its short length, ring-protected structure, and lipid modification, the construct demonstrated improved proteolytic stability against chymotrypsin, trypsin and protease K. Our findings suggest that optimizing lipid-peptide combinations can lead to more effective, specific, and stable candidates for antimicrobial development.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13596117/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149026494","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"PrismaLuc luciferase enables tunable near-infrared bioluminescence for <i>in vivo</i> imaging.","authors":"Felipe Gama-Franceschi, Rachel Friedman Ohana, Chao Gao, Thomas Kirkland, Laura Mezzanotte","doi":"10.1039/d6cb00175k","DOIUrl":"10.1039/d6cb00175k","url":null,"abstract":"<p><p>Bioluminescence imaging (BLI) enables non-invasive monitoring of biological processes in living animals, yet most bioluminescent reporters emit at fixed wavelengths with limited spectral flexibility, constraining their use in multiplexed and deep-tissue applications. Bioluminescence resonance energy transfer (BRET) offers a solution by coupling a luciferase to a proximal fluorescent protein or synthetic fluorophore that absorbs the emitted light and re-emits it at a longer wavelength. However, existing BRET systems built from luciferase-fluorescent protein fusions are limited by suboptimal energy transfer efficiency and the fixed photophysical properties of their genetically encoded chromophores. We recently introduced PrismaLuc, a high-efficiency BRET reporter, in which a circularly permuted NanoLuc is inserted into HaloTag, enabling efficient energy transfer to a covalently bound synthetic fluorophore whose emission wavelength is selected by choice of ligand. In our initial report, PrismaLuc was paired with JF549 HaloTag ligand for two-colour cell-based assays. Here, we extend PrismaLuc to <i>in vivo</i> bioluminescence imaging using far-red and near-infrared HaloTag ligands. In cultured cells, labelling with JF608 and JF669 HaloTag ligands produced emission peaks at 640 and 690 nm, respectively. Direct comparison with established BRET reporters revealed greater photon output at wavelengths above 665 nm, which are less attenuated in tissue. In tumour-bearing mice, PrismaLuc:JF669 produced an emission peak of approximately 700 nm, and <i>in vivo</i> fluorescence imaging confirmed sufficient JF669 HaloTag ligand bioavailability to label PrismaLuc expressed in xenograft tumours. Finally, dual-colour imaging in mice co-implanted with NanoLuc- and PrismaLuc-expressing cells demonstrated clear spectral separation, enabling multiplexed detection within the same animal. Together, these results establish PrismaLuc as a tunable platform for near-infrared and dual-colour bioluminescence imaging <i>in vivo</i>.</p>","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13565418/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148956944","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}