ACS Chemical Neuroscience最新文献

{"title":"Selection of DNA Aptamers That Promote Neurite Outgrowth in Human iPSC-Derived Sensory Neuron Organoid Cultures","authors":"Brandon Wilbanks,&nbsp;Jenelle Rolli,&nbsp;Keenan Pearson,&nbsp;Sybil C. L. Hrstka,&nbsp;Ronald F. Hrstka,&nbsp;Arthur E. Warrington,&nbsp;Nathan P. Staff and L. James Maher III*,&nbsp;","doi":"10.1021/acschemneuro.5c0016210.1021/acschemneuro.5c00162","DOIUrl":"https://doi.org/10.1021/acschemneuro.5c00162https://doi.org/10.1021/acschemneuro.5c00162","url":null,"abstract":"<p >Sensory neurons in the dorsal root ganglia transmit sensory signals from the periphery to the central nervous system. Induced pluripotent stem cell derived models of sensory neurons and dorsal root ganglia are among the most advanced available tools for the study of sensory neuron activity and development in human genetic backgrounds. However, few available reagents modify sensory neuron growth with disease or other model-relevant outcomes. Small molecules, peptides, or oligonucleotides that predictably alter sensory neuron behavior in these contexts would be valuable tools with potentially wide-ranging application. Here we describe the selection and characterization of DNA aptamers that specifically interact with human sensory neurons. Several selected aptamers increase neurite outgrowth from sensory neuron organoid cultures after single-dose treatments.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1258–1263 1258–1263"},"PeriodicalIF":4.1,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acschemneuro.5c00162","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746160","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Identification and Characterization of the Structure and Size of Aβ42 Oligomers Targeting the Receptor FcγRIIb","authors":"Mengke Jia,&nbsp;Chuanbo Wang,&nbsp;Jinfei Mei,&nbsp;Sajjad Ahmad,&nbsp;Muhammad Fahad Nouman and Hongqi Ai*,&nbsp;","doi":"10.1021/acschemneuro.4c0086210.1021/acschemneuro.4c00862","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00862https://doi.org/10.1021/acschemneuro.4c00862","url":null,"abstract":"<p >Kam and colleagues discovered that FcγRIIb can specifically bind to Aβ42 oligomers (AβOs). The N-terminal residues F4 and D7 of Aβ42, as well as the W115 residue in domain D2 of FcγRIIb, are involved in this binding. However, the specificity of the FcγRIIb receptor’s binding sites for AβOs and their dependence on different AβO species, including dimers (D/D_T), trimers (T/T_T), tetramers (Te/Te_T), and pentamers (P/P_T) during both the primary (P1) and secondary nucleation phases (P2), remains unknown. To address this, we employed molecular dynamics (MD) simulations to investigate the interactions between the extracellular domains D1 and D2 (FDD) of FcγRIIb and AβOs of varying sizes in the two different phases. We discovered that three specific fragments (f1, f2, and f3) of domain D2 in FDD are the primary binding sites for AβO species. Furthermore, among AβOs of the same molecular weight, those from the P2 phase exhibit a stronger binding affinity for FDD than those from the P1 phase. The distinction is ascribed to the stronger dependence on the hydrophobic residues in the β1 and β2 regions for the binding of AβOs in P2 (including T_T, Te_T, and P_T) than that (including D, Te, and P) in the P1 phase. In the P1 phase, these AβOs prefer to achieve binding to FDD through their N-terminal residues; however, by this, we identified that the species observed in Kam’s experiment to bind FcγRIIb should probably be the tetrameric AβO (Te) in the P1 phase. Moreover, within both the P1 and P2 phases, we predicted that the trimeric AβO species in either the P1 or P2 phase is the strongest binding ligand for the FcγRIIb receptor. This study provides a comprehensive molecular perspective on the interaction between FcγRIIb and AβO in P2, which is of significant importance for the development of therapeutic strategies targeting Alzheimer’s disease (AD) and autoimmune diseases.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1335–1345 1335–1345"},"PeriodicalIF":4.1,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746159","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular Generation for CNS Drug Discovery and Design","authors":"Shengneng Chen,&nbsp;Ding Luo and Weiwei Xue*,&nbsp;","doi":"10.1021/acschemneuro.5c0009510.1021/acschemneuro.5c00095","DOIUrl":"https://doi.org/10.1021/acschemneuro.5c00095https://doi.org/10.1021/acschemneuro.5c00095","url":null,"abstract":"<p >Computational drug design is a rapidly evolving field, especially the latest breakthroughs in generative artificial intelligence (GenAI) to create new compounds. However, the potential of GenAI to address the challenges in designing central nervous system (CNS) drugs that can effectively cross the blood-brain barrier (BBB) and engage their targets remains largely unexplored. The integration of GenAI techniques with experimental data sets and advanced evaluation metrics provides a unique opportunity to enhance CNS drug discovery. In this viewpoint, we will introduce the definition of CNS drug-like properties and data resources in CNS drug discovery, highlighting the need to train specialized GenAI models aimed at designing novel CNS drug candidates by efficiently exploring the CNS drug-like space.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1247–1250 1247–1250"},"PeriodicalIF":4.1,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746025","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Evidence of α-Synuclein/Glucocerebrosidase Dual Targeting by Iminosugar Derivatives","authors":"Giuseppe Tagliaferro,&nbsp;Maria Giulia Davighi,&nbsp;Francesca Clemente*,&nbsp;Filippo Turchi,&nbsp;Marco Schiavina,&nbsp;Camilla Matassini,&nbsp;Andrea Goti,&nbsp;Amelia Morrone,&nbsp;Roberta Pierattelli*,&nbsp;Francesca Cardona* and Isabella C. Felli*,&nbsp;","doi":"10.1021/acschemneuro.4c0061810.1021/acschemneuro.4c00618","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00618https://doi.org/10.1021/acschemneuro.4c00618","url":null,"abstract":"<p >Intrinsically disordered proteins (IDPs) are highly flexible molecules often linked to the onset of incurable diseases. Despite their great therapeutic potential, IDPs are often considered as undruggable because they lack defined binding pockets, which constitute the basis of drug discovery approaches. However, small molecules that interact with the intrinsically disordered state of α-synuclein, the protein linked to Parkinson’s disease (PD), were recently identified and shown to act as chemical chaperones. Glucocerebrosidase (GCase) is an enzyme crucially involved in PD, since mutations that code for GCase are among the most frequent genetic risk factors for PD. Following the “dual-target” approach, stating that one carefully designed molecule can, in principle, interfere with more than one target, we identified a pharmacological chaperone for GCase that interacts with the intrinsically disordered monomeric form of α-synuclein. This result opens novel avenues to be explored in the search for molecules that act on dual targets, in particular, with challenging targets such as IDPs.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1251–1257 1251–1257"},"PeriodicalIF":4.1,"publicationDate":"2025-03-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acschemneuro.4c00618","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746026","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparative Radiotracing Quantifies Brain Cellular Uptake and Catabolism of Bispecific Antibodies Targeting Transferrin Receptor and CD98hc","authors":"Jacob L. Veire,&nbsp;Michael J. Lucas,&nbsp;Layne G. Bond,&nbsp;Deepika R. Tripu,&nbsp;Peter M. Tessier* and Colin F. Greineder*,&nbsp;","doi":"10.1021/acschemneuro.4c0055210.1021/acschemneuro.4c00552","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00552https://doi.org/10.1021/acschemneuro.4c00552","url":null,"abstract":"<p >Bispecific antibodies (bAbs) that engage cerebrovascular targets, induce transport across the blood-brain barrier (BBB), and redistribute to secondary targets within the brain parenchyma have the potential to transform the diagnosis and treatment of a wide range of central nervous system disorders. Full understanding of the pharmacokinetics (PK) of these agents, including their potential for delivering cargo into brain parenchymal cells, is a key priority for the development of numerous potential therapeutic applications. To date, the brain PK of bAbs that target transferrin receptor (TfR-1) and CD98 heavy chain (CD98hc) has been characterized using techniques incapable of distinguishing between CNS clearance of intact protein from uptake and catabolism by brain parenchymal cells. Herein, we address this knowledge gap via a comparative radiotracing strategy using two radioisotopes with distinct residualizing properties, iodine-125 (I-125) and zirconium-89 (Zr-89). We first identify reaction conditions for tetravalent chelator modification and Zr-89 radiolabeling that do not adversely affect <i>in vitro</i> or <i>in vivo</i> function. We then use comparative radiotracing to define the PK of TfR-1 and CD98hc targeted bAbs without a parenchymal target, generating quantitative evidence of TfR-1-mediated cellular uptake and catabolism that implicates these processes in previously reported differences in the brain retention of IgGs shuttled across the BBB via these two pathways. Finally, we perform comparative radiotracing on a TfR-1 bAb with an internalizing neuronal target (TrkB), demonstrating rapid divergence of Zr-89 and I-125 PK curves, with a &gt; 30-fold difference in brain content of the two radioisotopes. Together, these results establish comparative radiotracing as a valuable technique for identifying internalizing cellular targets within the brain parenchyma and quantifying the extent and timing of bAb uptake and catabolism following target engagement.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1264–1274 1264–1274"},"PeriodicalIF":4.1,"publicationDate":"2025-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746056","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploring the Potential of Indole-3-acetic Acid Arylhydrazone Hybrids for Parkinson’s Disease Treatment: A Comprehensive Evaluation of Neuroprotective, MAOB Inhibitory, and Antioxidant Properties","authors":"Neda Anastassova*,&nbsp;Magdalena Kondeva-Burdina,&nbsp;Nadya Hristova-Avakumova,&nbsp;Denitsa Stefanova,&nbsp;Miroslav Rangelov,&nbsp;Nadezhda Todorova and Denitsa Yancheva,&nbsp;","doi":"10.1021/acschemneuro.4c0083810.1021/acschemneuro.4c00838","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00838https://doi.org/10.1021/acschemneuro.4c00838","url":null,"abstract":"<p >In the current study, a small series of five indole-3-acetic acid-derived arylhydrazone hybrids were synthesized and subjected to comprehensive evaluation of their neuropharmacological and radical-scavenging properties. Minimal neurotoxic effects were observed across diverse subcellular fractions, with particular emphasis on the compound <b>3a</b> bearing a 2,3-dihydroxy moiety, exhibiting superior neuroprotective effects against H₂O₂-induced oxidative stress by preserving the cell viability up to 68%. Noteworthy neuroprotection was observed in 6-OHDA-induced neurotoxicity using isolated rat brain synaptosomes, with compounds <b>3b</b> and <b>3c</b> displaying prominent effects. Compound <b>3a</b> demonstrated robust neuroprotective and antioxidant effects in models of <i>tert</i>-butyl hydroperoxide-induced oxidative stress on isolated rat brain mitochondria and nonenzyme-induced lipid peroxidation using isolated rat brain microsomes (Fe/AA). All compounds exhibited MAOB inhibition within the range of 0.130–0.493 μM, with compounds <b>3d</b>, <b>3e</b>, and <b>3a</b> showing notable selectivity against hMAOB. Molecular docking studies further validated ligand binding within MAOB active sites. The derivatives demonstrated scavenging activity and antioxidant effects against various ROS types, with compound <b>3a</b> consistently exhibiting the most potent activity. Structural modifications exerted discernible effects on scavenging capabilities and antioxidant effects, underscoring their potential therapeutic implications in neuroprotection and oxidative stress mitigation.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 6","pages":"1161–1181 1161–1181"},"PeriodicalIF":4.1,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143641568","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A Brain-Penetrating Foldamer Rescues Aβ Aggregation-Associated Alzheimer’s Disease Phenotypes in In Vivo Models","authors":"Charles Zuwu Baysah,&nbsp;Ryan A. Dohoney,&nbsp;L. Palanikumar,&nbsp;Nicholas H. Stillman,&nbsp;Alexandra L. Penney,&nbsp;Andres D. Sola,&nbsp;Daniel A. Paredes,&nbsp;Mazin Magzoub and Sunil Kumar*,&nbsp;","doi":"10.1021/acschemneuro.4c0075310.1021/acschemneuro.4c00753","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00753https://doi.org/10.1021/acschemneuro.4c00753","url":null,"abstract":"<p >Alzheimer’s disease (AD) is a progressive neurodegenerative disorder that is the leading cause of dementia, affecting nearly 55 million people across the world. One of the central pathological factors associated with AD is the aggregation of Aβ₄₂, a peptide product cleaved through pathological processes in AD. Under pathological conditions, Aβ₄₂ aggregates into insoluble plaques in the brain and impairs the function of neurons, which contributes to the cognitive decline associated with AD. Therefore, the modulation of Aβ₄₂ aggregation is considered a potential therapeutic intervention for AD. Using an Oligoquinoline-based foldamer library, we have identified a potent foldamer antagonist (SK-131) of Aβ₄₂ aggregation. SK-131 inhibits the aggregation by inducing a α-helical structure in monomeric Aβ₄₂. Here, we demonstrated that SK-131 rescues Aβ₄₂ aggregation-associated phenotypes in AD cellular and multiple <i>Caenorhabditis elegans</i> AD models, including intracellular inhibition of Aβ₄₂ aggregation, rescue of behavioral deficits, and attenuation of reactive oxygen species. It efficiently crosses the blood–brain barrier and demonstrates favorable pharmaceutical properties. It also potently inhibits Zn²⁺-mediated Aβ₄₂ aggregation by potentially displacing Zn²⁺ from Aβ₄₂. In summary, we have identified a potent brain-penetrating foldamer that efficiently rescues AD phenotypes in <i>in vivo</i> models. Unlike most of the therapeutic approaches that target Aβ aggregates, we have identified and validated a novel therapeutic pathway by inducing structural change in Aβ and rescuing AD phenotypes in <i>in vivo</i> models. This study will further aid in the quest to identify lead therapeutics to slow or stop the progression of AD.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1309–1322 1309–1322"},"PeriodicalIF":4.1,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143745890","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Neurochemical Assessment of Tissue Levels of Neurotransmitters for Approximating Neurotransmitter System Connectivity","authors":"Jasmine Jade Butler,&nbsp;Chloé Aman,&nbsp;Marion Rivalan,&nbsp;Aurélie Fitoussi,&nbsp;Sandrine Parrot,&nbsp;Françoise Dellu-Hagedorn and Philippe De Deurwaerdère*,&nbsp;","doi":"10.1021/acschemneuro.5c0006010.1021/acschemneuro.5c00060","DOIUrl":"https://doi.org/10.1021/acschemneuro.5c00060https://doi.org/10.1021/acschemneuro.5c00060","url":null,"abstract":"<p >The post-mortem measurement of tissue neurotransmitters is an interesting technique to address the gross biochemical activity. Its primary limitation is a lack of temporal resolution, although this is mitigated by enhanced spatial resolution, compared to <i>in vivo</i> methods. This neurochemical data is quantitative and requires no complex transformation, making it ideal to analyze neurochemical connectivity via the correlation of the biochemical signals between brain regions. These correlative approaches to quantitative measurements are fundamentally based on the variability of the data, an underdeveloped area of analysis in neurochemistry. One of the main reasons, as discussed in this Viewpoint, is that neurochemists recognize that variability in quantitative data stems not only from the biological variability, such as interindividual differences, but also from factors such as analytical devices. There are several ways to reduce variability caused by analytical and experimental biases through well-designed, precise protocols, allowing for the study of meaningful biological variability, such as interindividual differences between subjects.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 7","pages":"1243–1246 1243–1246"},"PeriodicalIF":4.1,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143746054","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fluorescent Sensor for the Visualization of Amino Acid Neurotransmitters in Neurons Based on an SNAr Reaction","authors":"Ming Xu,&nbsp;Peeyush Yadav,&nbsp;Xin Liu,&nbsp;Kevin D. Gillis* and Timothy E. Glass*,&nbsp;","doi":"10.1021/acschemneuro.5c0010710.1021/acschemneuro.5c00107","DOIUrl":"https://doi.org/10.1021/acschemneuro.5c00107https://doi.org/10.1021/acschemneuro.5c00107","url":null,"abstract":"<p >Glutamate is an important excitatory neurotransmitter, while GABA is an inhibitory neurotransmitter. However, direct and accurate visualization of these important signaling agents by a chemical sensor is still very challenging. Here, a novel coumarin-based fluorescent sensor for the selective labeling and imaging of amino acids in neurons has been developed. This sensor system provides two binding sites for amino acids: an aldehyde group for the amine binding and a modified fluorobenzene for an unusual nucleophilic aromatic substitution (S_NAr) reaction of a carboxyl group. Spectroscopic studies reveal a large fluorescence enhancement upon reaction with glutamate. Compounds lacking both groups did not activate the sensor. A clear and efficient visualization of neurotransmitters in cultured hippocampus neurons was obtained by imaging studies.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 6","pages":"1238–1242 1238–1242"},"PeriodicalIF":4.1,"publicationDate":"2025-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143641567","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Radiosynthesis, In Vitro Characterization, and In Vivo PET Neuroimaging of [18F]F-4 for Tau Protein: A First-in-Human PET Study","authors":"Anton Lindberg,&nbsp;Junchao Tong,&nbsp;Chao Zheng,&nbsp;Andre Mueller,&nbsp;Heiko Kroth,&nbsp;Andrew Stephens,&nbsp;Chester A. Mathis and Neil Vasdev*,&nbsp;","doi":"10.1021/acschemneuro.4c0086610.1021/acschemneuro.4c00866","DOIUrl":"https://doi.org/10.1021/acschemneuro.4c00866https://doi.org/10.1021/acschemneuro.4c00866","url":null,"abstract":"<p >[¹⁸F]PI-2620 is a promising radiopharmaceutical for positron emission tomography (PET) imaging of both Alzheimer’s disease (AD) and non-Alzheimer’s disease (non-AD) tauopathies in humans. An array of fluorinated derivatives of the carbazole scaffold of PI-2620 were synthesized and evaluated. <i>In vitro</i> binding assays with [³H]PI-2620 in human tissues with AD, progressive supranuclear palsy, and corticobasal degeneration, combined with <i>in silico</i> predictions of blood–brain barrier permeability, led to the selection and radiosynthesis of [¹⁸F]F-4 as a promising radiotracer. <i>In vivo</i> PET imaging with [¹⁸F]F-4 in healthy rats showed brain uptake and kinetics suitable for neuroimaging, similar to those of [¹⁸F]PI-2620. A first-in-human PET imaging study in a healthy subject as well as a patient with AD, in comparison with [¹⁸F]PI-2620 in the same AD subject, confirmed that [¹⁸F]F-4 is an alternative radiopharmaceutical for imaging tau protein.</p>","PeriodicalId":13,"journal":{"name":"ACS Chemical Neuroscience","volume":"16 6","pages":"1182–1189 1182–1189"},"PeriodicalIF":4.1,"publicationDate":"2025-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acschemneuro.4c00866","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143641550","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}