{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,28]],"date-time":"2026-04-28T08:02:20Z","timestamp":1777363340088,"version":"3.51.4"},"reference-count":57,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2020,9,9]],"date-time":"2020-09-09T00:00:00Z","timestamp":1599609600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Neurochemistry"],"published-print":{"date-parts":[[2021,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:label\/><jats:p>Protein aggregation into amyloid fibrils is a key feature of a multitude of neurodegenerative diseases such as Alzheimer's, Parkinson's, and Prion disease. To detect amyloid fibrils, fluorophores with high sensitivity and better efficiency coupled with the low toxicity are in high demand even to date. In this pursuit, we have unveiled two benzimidazole\u2010based fluorescence sensors ([C<jats:sub>15<\/jats:sub>H<jats:sub>15<\/jats:sub>N<jats:sub>3<\/jats:sub>] (<jats:bold>C1<\/jats:bold>) and [C<jats:sub>16<\/jats:sub>H<jats:sub>16<\/jats:sub>N<jats:sub>3<\/jats:sub>O<jats:sub>2<\/jats:sub>] (<jats:bold>C2<\/jats:bold>), which possess exceptional affinity toward different amyloid fibrils in its submicromolar concentration (8\u00a0\u00d7\u00a010<jats:sup>\u20139<\/jats:sup>\u00a0M), whereas under a similar concentration, the gold standard Thioflavin\u2010T (ThT) fails to bind with amyloid fibrils. These fluorescent markers bind to \u03b1\u2010Syn amyloid fibrils as well as amyloid fibrils forming other proteins\/peptides including A\u03b242 amyloid fibrils. The <jats:sup>1<\/jats:sup>H\u2010<jats:sup>15<\/jats:sup>N heteronuclear quantum correlation spectroscopy nuclear magnetic resonance data collected on wild\u2010type \u03b1\u2010Syn monomer with and without the fluorophores (<jats:bold>C1<\/jats:bold> and <jats:bold>C2<\/jats:bold>) reveal that there is weak or no interactions between <jats:bold>C1<\/jats:bold> or <jats:bold>C2<\/jats:bold> with residues in \u03b1\u2010Syn monomer, which indirectly reflects the specific binding ability of <jats:bold>C1<\/jats:bold> and <jats:bold>C2<\/jats:bold> to the \u03b1\u2010Syn amyloid fibrils. Detailed studies further suggest that <jats:bold>C1<\/jats:bold> and <jats:bold>C2<\/jats:bold> can detect\/bind with the \u03b1\u2010Syn amyloid fibril as low as 100\u00a0\u00d7\u00a010<jats:sup>\u20139<\/jats:sup>\u00a0M. Extremely low or no cytotoxicity is observed for <jats:bold>C1<\/jats:bold> and <jats:bold>C2<\/jats:bold> and they do not interfere with \u03b1\u2010Syn fibrillation kinetics, unlike ThT. Both <jats:bold>C1<\/jats:bold>\/<jats:bold>C2<\/jats:bold> not only shows selective binding with amyloid fibrils forming various proteins\/peptides but also displays excellent affinity and selectivity toward \u03b1\u2010Syn amyloid aggregates in SH\u2010SY5Y cells and A\u03b242 amyloid plaques in animal brain tissues. Overall, our data show that the developed dyes could be used for the detection of amyloid fibrils including \u03b1\u2010Syn and A\u03b242 amyloids with higher sensitivity as compared to currently used ThT.<\/jats:p><\/jats:sec><jats:sec><jats:label\/><jats:p>\n<jats:boxed-text content-type=\"graphic\" position=\"anchor\"><jats:graphic xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" mimetype=\"image\/png\" position=\"anchor\" specific-use=\"enlarged-web-image\" xlink:href=\"graphic\/jnc15138-fig-0012-m.png\"><jats:alt-text>image<\/jats:alt-text><\/jats:graphic><\/jats:boxed-text>\n<\/jats:p><\/jats:sec>","DOI":"10.1111\/jnc.15138","type":"journal-article","created":{"date-parts":[[2020,8,4]],"date-time":"2020-08-04T21:17:01Z","timestamp":1596575821000},"page":"1003-1019","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":12,"title":["Benzimidazole\u2010based fluorophores for the detection of amyloid fibrils with higher sensitivity than Thioflavin\u2010T"],"prefix":"10.1111","volume":"156","author":[{"given":"Narayanaperumal","family":"Pravin","sequence":"first","affiliation":[{"name":"Department of Chemistry Indian Institute of Technology Bombay Mumbai Maharashtra India"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rakesh","family":"Kumar","sequence":"additional","affiliation":[{"name":"Department of Biosciences and Bioengineering Indian Institute of Technology Bombay Mumbai Maharashtra India"},{"name":"Division of Neurogeriatrics Department of Neurobiology, Care Sciences and Society Karolinska Institutet Stockholm Sweden"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shalini","family":"Tripathi","sequence":"additional","affiliation":[{"name":"Department of Chemistry Indian Institute of Technology Bombay Mumbai Maharashtra 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