ACS Bio & Med Chem Au最新文献

{"title":"Blue Fluorescent Siloxytecans Exhibit Potent Anticancer Activity and Enable Direct Real-Time Quantification of Intracellular Uptake","authors":"Isabella Lo,&nbsp;Sanika Vaidya,&nbsp;Ashley Mo,&nbsp;Alyssa Yee-Xin Chia,&nbsp;Katelyn Li,&nbsp;Jessica Parvin,&nbsp;Sripathy Sadagopan,&nbsp;Zane D’souza,&nbsp;Olivia Kwok,&nbsp;Jenny Zhang,&nbsp;Isa Baratoff,&nbsp;Shreya Somani,&nbsp;Lekhya Menta,&nbsp;Yining Xie,&nbsp;Thomas Sanchez,&nbsp;Terry Wang,&nbsp;Rebecca Chen,&nbsp;Akira Yamamoto,&nbsp;Joseph Pazzi,&nbsp;Edward Njoo","doi":"10.1021/acsbiomedchemau.5c00155","DOIUrl":"10.1021/acsbiomedchemau.5c00155","url":null,"abstract":"<p>Notwithstanding thenatural abundance of silicon on Earth,silicon-containingcompounds comprise relatively few pharmaceutical drugs, though severalsilylated natural products have demonstrated greater bioavailabilityand lipophilicity. Here, we apply this strategy in the preparationand biological evaluation of synthetic camptothecin analogs involvinga C-10 silyl ether on SN-38, which not only blocks a site of metabolismbut also enhances bright-blue fluorescence properties in such compounds.These siloxytecans exhibit comparable dose- and time-dependent antiproliferativeactivity in a broad panel of cancer cells. Uniquely, we demonstratethat the enhanced fluorescence of these compounds enables real-time,quantitative visualization of the dynamics and selectivity of intracellularuptake through fluorescence microscopy without the need for extensivesample preparation or installation of auxiliary fluorophores. We furtherdemonstrate that the kinetics of cellular uptake observed by fluorescencemicroscopy are consistent with time-course washout experiments withsubtle differences in anticancer potency in several cell lines. Furthercell cycle analysis by flow cytometry and cell-free topoisomeraseinhibition studies suggests that these siloxytecans retain the topoisomerase-inhibitingproperties of camptothecin and other related topoisomerase I inhibitors.Collectively, these studies highlight the utility of quantitativefluorescence microscopy in investigating mechanisms of biologicaltransport and the anticancer activity of such siloxytecans.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"1–14"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272094","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Photoinduced Electron Transfer Informs on Pathway Coupling in Flavin-Based Electron Bifurcation","authors":"Seth A. Wiley,&nbsp;Carolyn E. Lubner","doi":"10.1021/acsbiomedchemau.5c00232","DOIUrl":"10.1021/acsbiomedchemau.5c00232","url":null,"abstract":"<p>Flavin-based electron bifurcation (FBEB) is an enzymaticmechanismthat generates extremely high-energy electrons to drive unfavorablechemical reactions. It is utilized by the NADH-dependent ferredoxin:NADP⁺-oxidoreductase (Nfn) enzyme in hyperthermophile <em>Pyrococcusfuriosus</em> to bifurcate electrons from NADPH into the coupledlow-potential (endergonic) and high-potential (exergonic) pathways.This process enables <em>P. furiosus</em> to live in harshand uninviting environments. Despite its biological importance, themechanisms used by Nfn to facilitate exceptional directional controlover short-lived, high-energy electrons and to prevent undesired transfer,particularly along the low-potential pathway, are still not well understood.To elucidate how the protein environment contributes to electroniccontrol in the low-potential pathway, new techniques must be utilizedto probe these unstable intermediates. In this study, we have adaptedlow-temperature photoexcitation combined with electron paramagneticresonance (EPR) to accumulate the short-lived intermediate and placeit in the context of the other cofactors involved in the low-potentialpathway of Nfn. We observed coincident growth of both the radicalintermediate and its nearby [4Fe-4S] cluster over 4.5 h of illuminationwith NADPH at cryogenic temperatures. The photogenerated paramagneticspecies were stable in LN₂ storage indefinitely and recombinedwhen warmed to higher temperatures. The results provide insights intothe electron transfer steps and cofactor interactions along the lowpotential pathway, facilitating a more robust mechanistic understandingof the high-energy events of electron bifurcation. Furthermore, throughcomparison of cryogenic and room temperature experiments, a potentialgating step involving the movement of key residues important for thereversibility of electron flow along this pathway is suggested.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"78–89"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272114","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"mSumireF a Monomeric Violet Fluorescent Protein","authors":"Jacob Kress,&nbsp;Sookyeong Kim,&nbsp;Caitlynn Bryant,&nbsp;Emily Camila Lopez-Lopez,&nbsp;Jiali Zha,&nbsp;Mathew Tantama","doi":"10.1021/acsbiomedchemau.5c00175","DOIUrl":"10.1021/acsbiomedchemau.5c00175","url":null,"abstract":"<p>The development ofgenetically encoded labels for multicolor experimentsrequires a diverse palette of fluorescent proteins that are well-behaved.Here, we report mSumireF, a monomeric variant of the violet fluorescentprotein Sumire. On its own, the canonical monomerizing valine-to-lysinemutation at residue 206 causes a significant loss of brightness forthe mSumire variant. We found that brightness is recovered upon thereversion of mSumire’s tyrosine at position 165 back to phenylalanineas in its superfolder GFP grandparent. Importantly, this mSumireFvariant exhibits significantly less oligomerization tendency in theorganized smooth endoplasmic reticulum (OSER) assay in mammalian cellsand in protein solution assays. Furthermore, we demonstrate that anmSumireF donor can be effectively paired with the fluorescent proteinacceptors mCerulean3, mTurquoise2, and LSSmScarlet to generate FRET-basedATP biosensors. mSumireF thus provides an improved violet fluorescentprotein to expand color options with reduced concern of unwanted dimerization.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"36–43"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272103","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structural and Biochemical Characterization of Fusobacterium nucleatum Enoyl-ACP Reductase II (FabK) Reveals the Basis for Bacterial Species-Specific Inhibition","authors":"Kristiana Avad,&nbsp;Osama Alaidi,&nbsp;Destiny Okpomo,&nbsp;Fahad Bin Aziz Pavel,&nbsp;Darcy Doran,&nbsp;Madeline Matheson,&nbsp;Dianqing Sun,&nbsp;Julian Hurdle,&nbsp;Kirk E. Hevener","doi":"10.1021/acsbiomedchemau.5c00199","DOIUrl":"10.1021/acsbiomedchemau.5c00199","url":null,"abstract":"<p><em>Fusobacteriumnucleatum</em> is a Gram-negativeanaerobic bacterium ubiquitous in the oral cavity and increasinglyrecognized for its involvement in diverse clinical conditions, includingperiodontal disease, inflammatory bowel disease, premature birth,and several forms of cancer. These associations highlight the needfor narrow-spectrum antibacterial agents directed against <em>F. nucleatum</em> to avoid disruption of beneficial microfloraand limit the rise of antibiotic resistance. Recent studies have identifiedthe fusobacterial fatty acid synthesis pathway (FAS-II) enzyme, enoyl-acylcarrier protein (ACP) reductase, <em>Fn</em>FabK, as an essentialand promising target for selective antibacterial intervention. However,there is a lack of detailed structural information, which has hinderedthe validation of <em>Fn</em>FabK’s druggability andthe discovery of new inhibitors. Here, we present a comprehensivecharacterization of <em>Fn</em>FabK, including its cocrystalstructure solved at 2.25 Å resolution and its biochemical andbiophysical interactions with a series of potent small-molecule inhibitors.Our analyses revealed that these inhibitors display low to submicromolaractivity against <em>Fn</em>FabK, with notable selectivityand differential activity when tested against FabK homologues fromother bacterial pathogens. Importantly, the unique structural featuresof the <em>Fn</em>FabK active site, elucidated through thesecrystallographic studies, provide a mechanistic basis for species-specificinhibition. These findings not only validate <em>Fn</em>FabKas a druggable target but also furnish critical insights into thedesign of next-generation narrow-spectrum antibacterial agents.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"44–55"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272129","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"OBIMAP (One-Bead Interchain Multipeptide Assembly Platform)","authors":"Othman Al Musaimi,&nbsp;Daryl R. Williams","doi":"10.1021/acsbiomedchemau.5c00237","DOIUrl":"10.1021/acsbiomedchemau.5c00237","url":null,"abstract":"<p>A significant advancement in Merrifield’s classicsolid-phasepeptide synthesis (SPPS) that greatly expands the scope of accessiblepeptide structures is reported here. Building upon the one-bead, one-compound(OBOC) concept, this approach enables the simultaneous synthesis ofmultiple peptides on a single bead, followed by a novel solid-phaseinterchain assembly reaction to produce the final peptide product.This method, the one-bead interchain multipeptide assembly platform(OBIMAP), successfully generates diverse peptide architectures, includinglinear, cyclic, and bicyclic structures<span></span>ranging from minimalcyclic dipeptides to small proteins<span></span>many of which are inaccessiblethrough conventional SPPS. OBIMAP demonstrates superior efficiencyin both time and product purity compared to traditional methods. Crucially,it eliminates the need for solution-phase fragment condensation, acommon but cumbersome step commonly used in synthesizing therapeuticpeptides (30–60 amino acids). In addition to enhancing conventionalSPPS methodologies, the OBIMAP enables access to novel classes ofpeptide architectures, including highly constrained peptides thatwere previously considered synthetically inaccessible.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"90–100"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272084","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Is Thiourea the Weak Link? An Investigation of the In Vitro and In Vivo Destabilization of [203Pb]- and [212Pb]Pb2+ Thiourea-Based Bioconjugates","authors":"Brooke L. McNeil,&nbsp;Luke Wharton,&nbsp;Chao-Cheng Chen,&nbsp;Helen Merkens,&nbsp;Milena Čolović,&nbsp;Cristina Rodríguez-Rodríguez,&nbsp;John Wilson,&nbsp;Stefan Mair,&nbsp;Chengcheng Zhang,&nbsp;Anthony W. McDonagh,&nbsp;Kuo-Shyan Lin,&nbsp;François Bénard,&nbsp;Frank Wuest,&nbsp;Paul Schaffer,&nbsp;Caterina F. Ramogida","doi":"10.1021/acsbiomedchemau.5c00224","DOIUrl":"10.1021/acsbiomedchemau.5c00224","url":null,"abstract":"<p>Fibroblast activationprotein (FAP) is overexpressedin a varietyof cancers, making it an attractive target for bifunctional chelator-basedradiopharmaceuticals. This study initially aimed to assess the effectof chelator structure on the biodistribution of ²⁰³Pb/²¹²Pb-labeled FAP inhibitor (FAPI) bioconjugates. However,suboptimal in vivo biodistribution and imaging results suggested thebioconjugate was unstable. RadioHPLC analysis of urine samples suggestthe thiourea bond, formed during conjugation between an amine on thebiomolecule, and an isothiocyanate-functionalized chelator, is unstablein vivo, resulting in detachment of the radiometal-chelator complexfrom the targeting vector, resulting in poor tumor accumulation. Todetermine whether this instability was specific to the FAPI system,a peptide-based (Cyclic melanocyte stimulating hormone, CycMSH) bioconjugatetargeting the melanocortin-1 receptor was synthesized using the samethiourea linkage. Identical metabolites were observed, supportingthe hypothesis that thiourea bonds are unstable in vivo with thistheranostic isotope pair. Subsequently, the effect of bioconjugationchemistry, specifically thiourea and amide bonds, on the stabilityand biodistribution of ²⁰³Pb/²¹²Pb-labeled bioconjugateswas assessed. Modifying the bioconjugation linker to be an amide bond,formed by utilizing a chelate containing an active ester instead ofan isothiocyanate, led to significantly improved in vitro and in vivostability, as demonstrated by radioHPLC and biodistribution and imagingstudies in both models. These findings highlight the importance ofthe choice of bioconjugation chemistry in the development of lead-basedradiopharmaceuticals and emphasize the importance of selecting stablelinkages to ensure optimal radiometal retention and tumor targeting.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"6 1","pages":"56–77"},"PeriodicalIF":3.5,"publicationDate":"2026-02-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147272077","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Tutorial Review on Surface Plasmon Resonance Biosensors: Applications in Biomedicine.","authors":"Antony Chirco, Elisabetta Meacci, Giancarlo Margheri","doi":"10.1021/acsbiomedchemau.5c00182","DOIUrl":"10.1021/acsbiomedchemau.5c00182","url":null,"abstract":"<p><p>Surface Plasmon Resonance (SPR) has proven to be one of the most effective technologies in terms of specificity, affinity, and determination of kinetic parameters for evaluating interactions between macromolecules. The focus of this tutorial is to give an overview of the recent advances and applications of SPR biosensors in biomedicine that are presented emphasizing the potentiality for the detection of very low abundant compounds, which, in recent years, have assumed great importance for prevention and early diagnosis of various diseases in biomedicine. The real-time detection of important biomarkers such as tumor markers, viruses, and toxins but also of compounds of interest such as drugs and hormones allows point-of-care analysis and monitoring of disease progression quickly and in a less invasive manner. Over the past years, several technical innovations have been introduced to SPR devices, which have gone through a process of miniaturization, portability, flexibility, and cost reduction. These characteristics are in line with the advantages of SPR biosensors over other biosensing techniques, i.e., to be label-free detection systems and their capacity to observe in real-time the interactions between a variety of molecules of interest at the metal surface. Recent advances in SPR sensor technology, such as LSPR, SPRi, and SPRM, attempted to improve the sensitivity and performance of molecule detection.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"5 6","pages":"922-946"},"PeriodicalIF":4.3,"publicationDate":"2025-11-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12715632/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145805727","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":"Photoactivatable, Biomimetic Ligand photoMultiTASQ Traps DNA/RNA G‑Quadruplexes and Their Protein Binding Partners.","authors":"Sandy Raevens, Yehuda M Danino, Cécile Desingle, Francesco Rota Sperti, Marc Pirrotta, Lucie Mazzucotelli, Léa Letissier, Eran Hornstein, Sarah Cianferani, Oscar Hernandez-Alba, Ibai E Valverde, David Monchaud","doi":"10.1021/acsbiomedchemau.5c00162","DOIUrl":"10.1021/acsbiomedchemau.5c00162","url":null,"abstract":"<p><p>The biological role of DNA and RNA G-quadruplexes (G4s) is relayed to the cellular circuitry by a plethora of proteins known as G4-binding proteins (G4PBs). It is thus critical to decipher the formation of the G4/G4BP complexes to accurately understand their involvement in G4-mediated regulatory mechanisms. While hundreds of G4-interacting compounds (G4 ligands) have been used to uncover G4 biology in a rather indirect manner, only a handful of multivalent ligands allowing for identifying associated proteins have been designed, mostly relying on the covalent capture of G4BPs upon photoactivation. We report herein on such a multivalent ligand named photoMultiTASQ, which belongs to a family of biomimetic and smart G4 ligands known as template-assembled synthetic G-quartets (TASQs). We show how photoMultiTASQ interacts with and photo-cross-links both DNA/RNA G4s and related G4BPs, and develop a new mass spectrometry (MS)-based technique to characterize the covalent adducts. Collectively, these results make photoMultiTASQ a new molecular tool in the arsenal of chemical cross-linking and isolation by pull-down (Chem-CLIP) technologies that uniquely identify targets and validate target engagement in cells.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"5 6","pages":"994-1006"},"PeriodicalIF":4.3,"publicationDate":"2025-10-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12715623/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145805782","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":"Manipulation of 7‑Finger Zinc Finger Nuclease Increases the Efficiency of Genome Editing in Human Cells.","authors":"Shota Katayama, Masahiro Watanabe, Wataru Nomura, Takashi Yamamoto","doi":"10.1021/acsbiomedchemau.5c00174","DOIUrl":"10.1021/acsbiomedchemau.5c00174","url":null,"abstract":"<p><p>Genome editing tools have great potential for medicinal use. Among them, zinc finger nucleases (ZFNs) are smaller in size than transcriptional activator-like effector nucleases and CRISPR-Cas9. Therefore, ZFNs are easily packed into a viral vector with limited cargo space, including adeno-associated viral vectors. Furthermore, because ZFN patents expired in 2020, high patent royalties are not required for application. Although functional 6-finger ZFNs can be easily prepared by modular assembly, it has been extremely difficult to produce functional 7-finger ZFNs, which are expected to have higher target specificity than 6-finger ZFNs in some cases. Herein we describe the construction of 7-finger ZFNs and the improvement in genome editing efficiency, which is generally lower in 7-finger ZFNs than in 6-finger ZFNs. Modular assembly of 7-finger ZFNs was achieved using a specific mutation, and the original genome editing efficiency was increased by up to 19%. Furthermore, 7-finger ZFNs showed reduced off-target effects, exhibiting higher target specificity than the corresponding 6-finger ZFNs. Our study provides critical insights for safer and more specific genome editing.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"5 6","pages":"1016-1026"},"PeriodicalIF":4.3,"publicationDate":"2025-10-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12715528/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145805737","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":"Leader-Independent C‑Terminal Modification by a Radical <i>S</i>‑Adenosyl‑l‑methionine Maturase Enables Macrocyclic GLP-1-Like Peptides.","authors":"Jacob K Pedigo, Karsten A S Eastman, Vahe Bandarian","doi":"10.1021/acsbiomedchemau.5c00152","DOIUrl":"10.1021/acsbiomedchemau.5c00152","url":null,"abstract":"<p><p>Ribosomally synthesized and post-translationally modified peptides (RiPPs) are a rapidly expanding family of natural products in which biosynthetic maturase enzymes tailor ribosomal precursors into bioactive products. Classical RiPP maturation relies on an N-terminal leader sequence in the precursor peptide and a complementary RiPP-recognition element in the enzyme to guide substrate binding. Herein, we interrogated PapB, a radical <i>S</i>-adenosyl-l-methionine RiPP maturase known to introduce thio-(seleno)-ether cross-links and discovered that its catalytic reach extends well beyond this paradigm. PapB efficiently processes substrates that lack any canonical leader sequence, demonstrating <i>bona fide</i> leader-independent activity. To highlight the practical value of this capability, we applied PapB to three therapeutically relevant analogues of glucagon-like peptide pathway agonists to generate C-terminal cyclic structures. In every case, the enzyme achieved complete conversion of the linear to the thioether macrocyclized peptide. These results establish PapB as a versatile, plug-and-play biocatalyst for late-stage macrocyclization of structurally diverse peptides, opening a direct route to conformationally constrained therapeutic candidates without the need for leader tags.</p>","PeriodicalId":29802,"journal":{"name":"ACS Bio & Med Chem Au","volume":"5 6","pages":"1007-1015"},"PeriodicalIF":3.5,"publicationDate":"2025-10-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12715619/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145805813","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}