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10.1021/acssensors.1c00518 http://scihub22266oqcxt.onion/10.1021/acssensors.1c00518 34038103!8375416!34038103     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=34038103&cmd=llinks): Failed to open stream: HTTP request failed! 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Activatable Carbocyanine Dimers for Photoacoustic and Fluorescent Detection of Protease Activity |pdf=|usr=}}{{34038103}} gab.com Text Activatable Carbocyanine Dimers for Photoacoustic and Fluorescent Detection of Protease Activity JO: ACS Sens http://www.kidney.de/pget.php?&tw=1&pmid=34038103 #FOAvip Activatable contrast agents are of ongoing research interest because they offer low background and high specificity to the imaging target. Engineered sensitivity to protease activity is particularly desirable because proteases are critical biomarkers in cancer, infectious disease, inflammatory disorders, and so forth. Herein, we developed and characterized a set of peptide-linked cyanine conjugates for dual-modal detection of protease activity via photoacoustic (PA) and fluorescence imaging. The peptide-dye conjugates were designed to undergo contact quenching via intramolecular dimerization and contained n dyes (n = 2, 3, or 4) with n - 1 cleavable peptide substrates. The absorption peaks of the conjugates were blue-shifted 50 nm relative to the free dye and had quenched fluorescence. This effect was sensitive to solvent polarity and could be reversed by solvent switching from water to dimethyl sulfoxide. Employing trypsin as a model protease, we observed a 2.5-fold recovery of the peak absorbance, 330-4600-fold fluorescent enhancement, and picomolar detection limits following proteolysis. The dimer probe was further characterized for PA activation. Proteolysis released single dye-peptide fragments that produced a 5-fold PA enhancement through the increased absorption at 680 nm with nanomolar sensitivity to trypsin. The peptide substrate could also be tuned for protease selectivity; as a proof-of-concept, we detected the main protease (M(pro)) associated with the viral replication in SARS-CoV-2 infection. Last, the activated probe was imaged subcutaneously in mice and signal was linearly correlated to the cleaved probe. Overall, these results demonstrate a tunable scaffold for the PA molecular imaging of protease activity with potential value in areas such as disease monitoring, tumor imaging, intraoperative imaging, in vitro diagnostics, and point-of-care sensing. Twit Text FOAVip Activatable Carbocyanine Dimers for Photoacoustic and Fluorescent Detection of Protease Activity ????ACS Sens http://www.kidney.de/pget.php?&tw=1&pmid=34038103 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34038103 #FOAvip English Wikipedia <ref>{{Cite pmid|34038103}}</ref> Activatable Carbocyanine Dimers for Photoacoustic and Fluorescent Detection of Protease Activity #MMPMID34038103 Moore C; Borum RM; Mantri Y; Xu M; Fajtova P; O'Donoghue AJ; Jokerst JV ACS Sens 2021[Jun]; 6 (6): 2356-2365 PMID34038103show ga Activatable contrast agents are of ongoing research interest because they offer low background and high specificity to the imaging target. Engineered sensitivity to protease activity is particularly desirable because proteases are critical biomarkers in cancer, infectious disease, inflammatory disorders, and so forth. Herein, we developed and characterized a set of peptide-linked cyanine conjugates for dual-modal detection of protease activity via photoacoustic (PA) and fluorescence imaging. The peptide-dye conjugates were designed to undergo contact quenching via intramolecular dimerization and contained n dyes (n = 2, 3, or 4) with n - 1 cleavable peptide substrates. The absorption peaks of the conjugates were blue-shifted 50 nm relative to the free dye and had quenched fluorescence. This effect was sensitive to solvent polarity and could be reversed by solvent switching from water to dimethyl sulfoxide. Employing trypsin as a model protease, we observed a 2.5-fold recovery of the peak absorbance, 330-4600-fold fluorescent enhancement, and picomolar detection limits following proteolysis. The dimer probe was further characterized for PA activation. Proteolysis released single dye-peptide fragments that produced a 5-fold PA enhancement through the increased absorption at 680 nm with nanomolar sensitivity to trypsin. The peptide substrate could also be tuned for protease selectivity; as a proof-of-concept, we detected the main protease (M(pro)) associated with the viral replication in SARS-CoV-2 infection. Last, the activated probe was imaged subcutaneously in mice and signal was linearly correlated to the cleaved probe. Overall, these results demonstrate a tunable scaffold for the PA molecular imaging of protease activity with potential value in areas such as disease monitoring, tumor imaging, intraoperative imaging, in vitro diagnostics, and point-of-care sensing. |*COVID-19[MESH] |*Photoacoustic Techniques[MESH] |Animals[MESH] |Carbocyanines[MESH] |Fluorescent Dyes[MESH] |Humans[MESH] |Mice[MESH] |Peptide Hydrolases/metabolism[MESH] |Proteolysis[MESH]Activatable Carbocyanine Dimers for Photoacoustic and Fluorescent Dete(epmc).pdf DeepDyve Pubget Overpricing