In vivo cell tracking has emerged as a much sought after tool for design and monitoring of cell-based treatment strategies. Various techniques are available for pre-clinical animal studies, from which much has been learned and still can be learned. However, there is also a need for clinically translatable techniques. Central to in vivo cell imaging is labelling of cells with agents that can give rise to signals in vivo, that can be detected and measured non-invasively. The current imaging technology of choice for clinical translation is MRI in combination with labelling of cells with magnetic agents. The main challenge encountered during the cell labelling procedure is to efficiently incorporate the label into the cell, such that the labelled cells can be imaged at high sensitivity for prolonged periods of time, without the labelling process affecting the functionality of the cells. In this respect, nanoparticles offer attractive features since their structure and chemical properties can be modified to facilitate cellular incorporation and because they can carry a high payload of the relevant label into cells. While these technologies have already been applied in clinical trials and have increased the understanding of cell-based therapy mechanism, many challenges are still faced.
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http://dx.doi.org/10.1259/bjr.20150375 | DOI Listing |
Angew Chem Int Ed Engl
January 2025
East China University of Science and Technology, Insitute of Fine Chemicals, Meilong Road 130, Shanghai, China, 200237, Shanghai, CHINA.
Protein clustering/disassembling is a fundamental process in biomolecular condensates, playing crucial roles in cell fate decision and cellular homeostasis. However, the inherent features of protein clustering, especially for its reversible behavior and subtle microenvironment variation, present significant hurdles in probe chemistry for tracking protein clustering dynamics. Herein, we report a bilateral-tailored chemigenetic probe, in which an "amphiphilic" AIEgen QMSO3Cl is covalently conjugated to a protein tag that is genetically fused to protein-of-interest (POI).
View Article and Find Full Text PDFHeliyon
January 2025
The Institute for Drug Research of the School of Pharmacy, Faculty of Medicine, The Hebrew University of Jerusalem, Jerusalem, Israel.
RNA-targeting small molecules, particularly RIBOnuclease TArgeting Chimeras (RIBOTACs), represent a powerful and promising therapeutic approach by selectively degrading RNAs through ribonuclease (RNase) recruitment. Despite their potential, the development of effective RNase recruitment tools is still in its early stages and remains a critical area of research. Ribonuclease L (RNase L) is a key ribonuclease targeted by RIBOTACs, yet the tools available for studying RNase L are limited.
View Article and Find Full Text PDFJ Extracell Biol
January 2025
Cell Biology Unit & Platform for Imaging Cells and Tissues, de Duve Institute UCLouvain Brussels Belgium.
The extracellular vesicle release in red blood cell concentrates reflects progressive accumulation of storage lesions and could represent a new measure to be implemented routinely in blood centres in addition to haemolysis. Nevertheless, there is currently no standardized isolation protocol. In a previous publication, we developed a reproducible ultracentrifugation-based protocol (20,000 × protocol) that allows to classify red blood cell concentrates into three cohorts according to their vesiculation level.
View Article and Find Full Text PDFRSC Chem Biol
January 2025
School of Chemistry, Advanced Research Centre, University of Glasgow 11 Chapel Lane Glasgow G11 6EW UK
Peptide stapling is an effective strategy to stabilise α-helical peptides, enhancing their bioactive conformation and improving physiochemical properties. In this study, we apply our novel diyne-girder stapling approach to the MDM2/MDMX α-helical binding region of the p53 transactivation domain. By incorporation of an unnatural amino acid to create an optimal , + 7 bridge length, we developed a highly α-helical stapled peptide, 4, confirmed circular dichroism.
View Article and Find Full Text PDFNatl Sci Rev
February 2025
Key Laboratory for Advanced Materials and Joint International Research Laboratory of Precision Chemistry and Molecular Engineering, Frontiers Science Center for Materiobiology and Dynamic Chemistry, School of Chemistry and Molecular Engineering, East China University of Science and Technology, Shanghai 200237, China.
Organic red/near-infrared (NIR) room-temperature phosphorescence (RTP) holds significant potential for autofluorescence-free bioimaging and biosensing due to its prolonged persistent luminescence and exceptional penetrability. However, achieving activatable red/NIR organic RTP probes with tunable emission in aqueous solution remains a formidable challenge. Here we report on aqueous organic RTP probes with red/NIR phosphorescence intensity and lifetime amplification.
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