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The identification of the dyes present on a linen fragment from the tomb of Pharaoh Tutankhamun is the objective of the present study. Fiber optic reflectance spectroscopy (FORS) was applied to the archaeological sample for preliminary identification of the dyes and to better choose the extraction methodology for different areas of the sample. The innovative gel-supported micro-extraction with agar gel and the Nanorestore Gel High Water Retention (HWR) gel were applied to the archaeological sample after testing of the best concentration for the extraction of the agar gels substrates, performed on laboratory mock-ups by means of UV-Vis transmittance spectroscopy. Immediately after extraction, Ag colloidal pastes were applied on the gel surface and Surface Enhanced Raman Scattering (SERS) analysis was performed directly on them. The combination of information deriving from FORS and SERS spectra resulted in the successful identification of both indigo and madder and, in hypothesis, of their degradation products.
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http://dx.doi.org/10.3390/gels9070514 | DOI Listing |
J Org Chem
September 2025
School of Chemical and Biopharmaceutical Sciences, Technological University Dublin, City Campus, Grangegorman, Dublin D07 EWV4, Ireland.
A series of unsymmetrically substituted BODIPY dyes featuring fused benzo- or naphtho-fragments on one pyrrolic unit were synthesized from the corresponding pyrrolic precursors. The synthetic route was optimized using a modular approach based on the condensation of formylpyrroles with alkylpyrroles, enabling the identification of precursor combinations that minimize byproduct formation and improve preparative yields. The resulting benzo- and naphtho-fused BODIPYs display intense fluorescence in the red region, with emission maxima spanning 590-680 nm and fluorescence quantum yields ranging from 0.
View Article and Find Full Text PDFInt J Nanomedicine
September 2025
Department of Orthopedics, Honghui Hospital, Xi'an Jiaotong University, Xi'an, Shaanxi, People's Republic of China.
Peptide-based fluorescent probes have found widespread applications in biomedical research, including bio-imaging, disease diagnosis, drug discovery, and image-guided surgery. Their favorable properties-such as small molecular size, low toxicity, minimal immunogenicity, and high targeting specificity-have contributed to their growing utility in both basic research and translational medicine. This review provides a comprehensive overview of recent advances in peptide-based fluorescent probes, emphasizing design strategies, biological targets, and diverse functional applications.
View Article and Find Full Text PDFFront Immunol
September 2025
Department of Biology, College of Science, United Arab Emirates University, Al Ain, United Arab Emirates.
Curcumin (1,7-bis-(4-hydroxy-3-methoxyphenyl)-hepta-1,6-diene-3,5-dione) is a naturally occurring polyphenol molecule. It is lipophilic and has demonstrated and therapeutic effects through multiple pathways. Extensive studies on its pharmacological properties have shown its anti-inflammatory, antioxidant, antinociceptive, antimicrobial, antiparasitic, antimalarial, and wound-healing properties.
View Article and Find Full Text PDFChem Pharm Bull (Tokyo)
September 2025
Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.
Antigen-binding proteins, such as nanobodies, modified with functional small molecules hold great potential for applications including imaging probes, drug conjugates, and localized catalysts. However, traditional chemical labeling methods that randomly target lysine or cysteine residues often produce heterogeneous conjugates with limited reproducibility. Conventional site-specific conjugation approaches, which typically modify only the N- or C-terminus, may also be insufficient to achieve the desired functionalities.
View Article and Find Full Text PDFNat Commun
August 2025
School of Pharmaceutical Sciences, MOE Key Laboratory of Bioorganic Phosphorus Chemistry & Chemical Biology, Beijing Frontier Research Center for Biological Structure, Tsinghua University, Beijing, China.
Advancement in fluorescence imaging techniques enables the study of protein dynamics and localization with unprecedented spatiotemporal resolution. However, current imaging tools are unable to elucidate dynamic protein interactomes underlying imaging observations. Conversely, proteomics tools such as proximity labeling enable the analysis of protein interactomes at a single time point but lack information about protein dynamics.
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