RSC Chemical Biology最新文献

ARCaDia-selected short DNA core positions a latent warhead for protein-gated covalent capture. arcadia选择的短DNA核心定位潜伏弹头，用于蛋白质门控共价捕获。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-16 DOI: 10.1039/d6cb00303f

Chaohui Li, Naoyuki Miyashita, Masayasu Kuwahara, Jay Yang, Masumi Taki

引用次数: 0

Solution structure of a peptide-conjugated aggregation-induced-emission (AIE) fluorophore bound to a protein. 结合蛋白的肽共轭聚集诱导发射（AIE）荧光团的溶液结构。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-15 DOI: 10.1039/d6cb00109b

Daniel Seifert, Matthias Hayduk, Torsten Herrmann, David Podlesainski, Jill Rohde, Jürgen Linders, Markus Kaiser, Peter Bayer, Jens Voskuhl, Christine Beuck

{"title":"Solution structure of a peptide-conjugated aggregation-induced-emission (AIE) fluorophore bound to a protein.","authors":"Daniel Seifert, Matthias Hayduk, Torsten Herrmann, David Podlesainski, Jill Rohde, Jürgen Linders, Markus Kaiser, Peter Bayer, Jens Voskuhl, Christine Beuck","doi":"10.1039/d6cb00109b","DOIUrl":"10.1039/d6cb00109b","url":null,"abstract":"Here, we present a class of peptide-conjugated fluorophores based on aromatic thioethers with aggregation-induced emission (AIE) properties for specific recognition of small proteins and also the first solution NMR structure of an AIE ligand specifically bound to a protein. Binding of the hPin1-WW domain as a model protein resulted in a significant fluorescence increase, making these AIE-peptide fluorophores suitable as direct readout probes for specific protein interactions. Autofluorescence and protein-binding properties were elucidated as a function of peptide length and fluorophore concentration. While an AIE fluorophore with two conjugated peptides shows an enhanced fluorescence increase upon protein binding, a one-armed derivative enabled us to solve the structures of the free AIE-peptide and its complex. In the absence of a protein, the AIE-peptide conjugate shows a curled-up conformation that still allows rotation of the aromatic rings of the AIE-core, thus resulting in low auto-fluorescence. In contrast, the AIE-peptide unfurls upon binding, allowing the hPin1-WW domain to interact with its peptide recognition sequence. The aromatic rings of the AIE-core form additional contacts with the protein surface, which restricts their motions and thus results in the observed fluorescence increase.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-10-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13670144/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149217048","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}

引用次数: 0

Correction: A biparatopic HER2-targeting ADC constructed via site-specific glycan conjugation exhibits superior stability, safety, and efficacy. 更正：通过位点特异性聚糖偶联构建的双异位her2靶向ADC具有优越的稳定性、安全性和有效性。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-09 DOI: 10.1039/d6cb90040b

Qi Xue, Jianjian Peng, Wenying Dai, Qingsong Wu, Jinbiao Jiao, Yudi Hu, Wanxing Sha, Yang Yang, Wenhao Yu, Siyang Liu, Ting Xu, Jie P Li

引用次数: 0

NAD⁺ analogues for decoding the biological chemistry of PARP-mediated ADP-ribosylation. 解码parp介导的adp核糖基化生物化学的NAD+类似物。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-09 DOI: 10.1039/d6cb00270f

Lijuan Gao, Yangyang Zhou, Tianye Dai, Yanhui Xu, Jing You, Jiahua Jiang, Xiao-Nan Zhang, Baohua Zhao

引用次数: 0

Exploring the biocatalytic potential of wild-type split transketolases. 探索野生型裂解转酮酶的生物催化潜力。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-07 DOI: 10.1039/d6cb00243a

Alessia Tonoli, Silvia Anselmi, Yeke Ni, John M Ward, Helen C Hailes, Jack W E Jeffries

引用次数: 0

Exploring RiPP-derived N-acyltransferases for genetically encoded lipopeptide engineering. 探索ripp衍生的n -酰基转移酶用于基因编码脂肽工程。

IF 3.9

RSC Chemical Biology Pub Date : 2026-10-06 DOI: 10.1039/d6cb00169f

Nina M Bösch, Manon Coste, Johannes A Rudmann Eckert, Gabriel Cervera Arriaga, Annina R Meyer, Eléonore Moore, Daniel Richter, Jörn Piel, Anna L Vagstad

{"title":"Exploring RiPP-derived N-acyltransferases for genetically encoded lipopeptide engineering.","authors":"Nina M Bösch, Manon Coste, Johannes A Rudmann Eckert, Gabriel Cervera Arriaga, Annina R Meyer, Eléonore Moore, Daniel Richter, Jörn Piel, Anna L Vagstad","doi":"10.1039/d6cb00169f","DOIUrl":"10.1039/d6cb00169f","url":null,"abstract":"Lipopeptides possess diverse bioactivities with widespread uses as antimicrobial drugs and biosurfactants but their biosynthetic engineering remains challenging. Classical lipopeptides (such as daptomycin or surfactin) are biosynthesized by modular, non-ribosomal megasynthetases. An alternative streamlined route to lipopeptides are the ribosomally synthesized and post-translationally modified peptides (RiPPs) derived from gene-encoded precursor proteins. We recently characterized a novel class of post-translational modification enzymes in RiPPs that catalyze fatty acylation of ornithine and lysine side chains. The resulting lipopeptides were termed selidamides. To assess the use of selidamide N-acyltransferases as biocatalysts, we probed the peptide substrate specificity of the model lauroyl-transferase KspN from kamptornamide biosynthesis. Nearest-neighbor, lysine-scan, and truncation mutants demonstrated promiscuity for the peptide substrate. As a proof-of-concept toward designer lipopeptides using RiPP biosynthetic principles, we produced sequences mimicking bioactive non-ribosomal lipopeptides and tested their conversion by maturases from the kamptornamide biosynthetic pathway. Ornithines, fatty acyl groups, and lanthionine macrocycles were installed in the mimics as a promising start toward the directed biosynthesis of custom lipopeptides.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13647313/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149138581","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}

引用次数: 0

High-throughput droplet screening of filamentous fungi on solid substrates. 丝状真菌在固体基质上的高通量液滴筛选。

IF 3.9

RSC Chemical Biology Pub Date : 2026-09-30 DOI: 10.1039/d6cb00197a

Chiara Leal Alves, Jeremy Z Wu, Elham Khanjani, Adiphol Dilokpimol, Zhiyang Deng, Biplu Prajapati, Niloufar Rahbari, Antti P Aalto, Mari Valkonen, Steve C C Shih

{"title":"High-throughput droplet screening of filamentous fungi on solid substrates.","authors":"Chiara Leal Alves, Jeremy Z Wu, Elham Khanjani, Adiphol Dilokpimol, Zhiyang Deng, Biplu Prajapati, Niloufar Rahbari, Antti P Aalto, Mari Valkonen, Steve C C Shih","doi":"10.1039/d6cb00197a","DOIUrl":"https://doi.org/10.1039/d6cb00197a","url":null,"abstract":"Droplet-based microfluidics has been frequently used for high-throughput single-cell microbial screening, where individual cells are encapsulated into nanoliter or picoliter-sized droplets and sorted based on measurable phenotypes such as fluorescent proteins or enzyme activity using fluorescence or absorbance-based substrates. However, using droplet microfluidics with filamentous fungi poses a unique challenge: fungal strains tend to escape from droplets as their hyphae grow, causing individual droplets to merge and eventually burst which prevents measuring individual phenotypes. In our work, we demonstrate a strategy to robustly encapsulate and retain spores of filamentous fungi within water-in-oil droplets by incorporating solid substrates into the droplet microenvironment. Using this approach, we show for the first time the encapsulation and growth of two model filamentous fungi species in droplets - Aspergillus oryzae and Trichoderma reesei - with solid substrates supporting spore retention, germination, and early hyphal development without compromising droplet stability. Our goal was to screen for enhanced enzyme production (e.g., α-amylase and cellulase) using fluorescence-based activity assays. To this end, we further characterized our top hits through scale-up fungal fermentation to evaluate improvements in both enzyme production and total protein secretion. Our work overcomes a key technical barrier in applying droplet microfluidics to filamentous fungi that allows for high-throughput screening and discovery of new fungal strains that produce active enzymes and heterologous proteins relevant to industrial applications.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13625276/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149116185","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}

引用次数: 0

Genetically encoded dinitrobenzyl photostabilizer for enhancing the photostability of fluorescent proteins. 提高荧光蛋白光稳定性的基因编码二硝基苯光稳定剂。

IF 3.9

RSC Chemical Biology Pub Date : 2026-09-29 DOI: 10.1039/d6cb00168h

Guihua Li, Xia Wang, Jiben Xue, Jie Wang

{"title":"Genetically encoded dinitrobenzyl photostabilizer for enhancing the photostability of fluorescent proteins.","authors":"Guihua Li, Xia Wang, Jiben Xue, Jie Wang","doi":"10.1039/d6cb00168h","DOIUrl":"10.1039/d6cb00168h","url":null,"abstract":"Fluorescent proteins (FPs) are essential tools for biological imaging, but their application in long-term and super-resolution microscopy is often limited by photobleaching. Inspired by \"self-healing\" organic dyes, we report a genetically encoded intramolecular photostabilization strategy to improve the ability of fluorescent proteins to resist photobleaching. We designed a dinitrobenzene-based unnatural amino acid (UAA), 2-NBAK, to function as an efficient photostabilizer. Using an engineered orthogonal translation system, we performed a systematic spatial scan of 192 insertion sites across the mNeonGreen (mNG) β-barrel. Our screening revealed that optimal mNG-2-NBAK variants at specific outward-pointing side chains are proposed to quench the triplet state without disrupting the chromophore emission spectra. In vitro characterization and further live-cell confocal imaging demonstrated that the optimal variants exhibited more than a twofold extension of the fluorescence half-life under intense continuous irradiation. By transplanting the optimal mNG insertion sites into another FP, we established a proof-of-concept for enhancing green FP photostability, providing a genetically encoded framework adaptable to other spectral variants with energetically matched photostabilizers.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13640607/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149116171","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}

引用次数: 0

"MIDA masking" of boronic acid therapeutics for enhanced stability and economy. 硼酸治疗的“MIDA掩蔽”增强稳定性和经济性。

IF 3.9

RSC Chemical Biology Pub Date : 2026-09-26 DOI: 10.1039/d6cb00308g

Forrest G FitzGerald, Jasmin M Frei, Erika Zhang, Oscar J Molina, JoLynn B Giancola, Malo Le Chevalier, Volga Kojasoy, Ronald T Raines

{"title":"\"MIDA masking\" of boronic acid therapeutics for enhanced stability and economy.","authors":"Forrest G FitzGerald, Jasmin M Frei, Erika Zhang, Oscar J Molina, JoLynn B Giancola, Malo Le Chevalier, Volga Kojasoy, Ronald T Raines","doi":"10.1039/d6cb00308g","DOIUrl":"https://doi.org/10.1039/d6cb00308g","url":null,"abstract":"Boronic acids are invaluable chemical reagents that enable the synthesis of complex organic molecules and are uniquely leveraged by medicinal chemists to target biological nucleophiles via an electrophilic boron center, thereby functioning as reversible covalent inhibitors. Despite their prevalence, boronic acids remain difficult to purify and are notoriously unstable in the presence of air, moisture, and reactive oxygen species-a major impediment to biological applications. We reasoned that the boronic acid protecting group N-methyliminodiacetic acid (MIDA), typically restricted to synthetic organic chemistry, could offer a superior protection strategy for boronic acid-containing bioactive molecules. Using the FDA-approved anticancer proteasome inhibitors bortezomib and ixazomib as proof-of-concept substrates, we demonstrate a several-hundred-fold increase in hydrolytic stability of a MIDA boronate compared to the current standard (e.g., diols and α-hydroxy acid protecting groups), imparting significant resistance to oxidation and photodegradation while minimally impacting the biological activity of the molecules in cellular assays. We propose that incorporating MIDA boronates into the synthetic routes of boronic acid-containing drugs could eliminate costly deprotection and reformulation steps in pharmaceutical development, enabling a more direct route to shelf-stable \"MIDA-masked\" boronic acid medicines.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13655787/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149184943","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}

引用次数: 0

Bioorthogonal chemistry for deciphering lipid biology in living systems. 生物正交化学用于解读生命系统中的脂质生物学。

IF 3.9

RSC Chemical Biology Pub Date : 2026-09-23 DOI: 10.1039/d6cb00259e

Brenda Portasany, Federica A Souto-Trinei, Roberto J Brea

{"title":"Bioorthogonal chemistry for deciphering lipid biology in living systems.","authors":"Brenda Portasany, Federica A Souto-Trinei, Roberto J Brea","doi":"10.1039/d6cb00259e","DOIUrl":"https://doi.org/10.1039/d6cb00259e","url":null,"abstract":"Lipids are among the most structurally diverse classes of biomolecules and play fundamental roles in membrane organization, energy storage, and cellular signalling. However, unlike proteins and nucleic acids, they are not directly encoded by the genome, making their selective visualization, manipulation, and functional interrogation in living systems particularly challenging. Over the past two decades, bioorthogonal chemistry has transformed lipid research by enabling the incorporation of minimally perturbing chemical reporters and the use of highly selective ligation reactions in complex biological environments. These advances have made it possible to synthesize, label, image, quantify, and manipulate lipids with unprecedented spatial and temporal precision. In this review, we discuss how bioorthogonal chemistry has expanded the experimental toolkit for deciphering lipid biology, highlighting applications ranging from the in situ synthesis of membrane-forming lipids and live-cell imaging to the investigation of lipid-protein interactions and the development of bioinspired therapeutic strategies. Finally, we discuss the remaining challenges and emerging opportunities for achieving a quantitative, dynamic, and spatially resolved understanding of lipid function in living systems.","PeriodicalId":40691,"journal":{"name":"RSC Chemical Biology","volume":" ","pages":""},"PeriodicalIF":3.9,"publicationDate":"2026-09-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13625287/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"149116119","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}

引用次数: 0