Discovery of <i>N</i>-(6-Methoxypyridin-3-yl)quinoline-2-amine Derivatives for Imaging Aggregated α-Synuclein in Parkinson’s Disease with Positron Emission Tomography

The fibrillary aggregation of α-synuclein is a hallmark of Parkinson’s disease (PD) and a potential target for diagnostics and therapeutics. Although substantial effort has been devoted to the development of positron emission tomography (PET) probes for detecting α-synuclein aggregates, no clinicall...

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Main Authors: Haiyang Zhao, Tianyu Huang, Dhruva D. Dhavale, Jennifer Y. O’Shea, Zsofia Lengyel-Zhand, Dinahlee Saturnino Guarino, Jiwei Gu, Xuyi Yue, Ying-Hwey Nai, Hao Jiang, Marshall G. Lougee, Vinayak V. Pagar, Hee Jong Kim, Benjamin A. Garcia, E. James Petersson, Chester A. Mathis, Paul T. Kotzbauer, Joel S. Perlmutter, Robert H. Mach, Zhude Tu
Format: Article
Language:English
Published: MDPI AG 2025-07-01
Series:Cells
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Online Access:https://www.mdpi.com/2073-4409/14/14/1108
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Summary:The fibrillary aggregation of α-synuclein is a hallmark of Parkinson’s disease (PD) and a potential target for diagnostics and therapeutics. Although substantial effort has been devoted to the development of positron emission tomography (PET) probes for detecting α-synuclein aggregates, no clinically suitable tracer has been reported. The design and synthesis of 43 new <i>N</i>-(6-methoxypyridin-3-yl)quinolin-2-amine derivatives and an evaluation of their α-synuclein binding affinity is reported here. Compounds <b>7f</b>, <b>7j</b>, and <b>8i</b> exhibited high affinity for α-synuclein and were selected for <sup>11</sup>C, <sup>18</sup>F, <sup>125</sup>I, or <sup>3</sup>H radiolabeling. A photoaffinity variant, <b>TZ-CLX</b>, structurally related to <b>7j</b> and <b>8i</b>, demonstrated preferential binding to the C-terminal region of α-synuclein fibrils. PET brain imaging studies using [<sup>11</sup>C]<b>7f</b>, [<sup>18</sup>F]<b>7j</b>, and [<sup>11</sup>C]<b>8i</b> in non-human primates indicated that these three α-synuclein PET tracers penetrated the blood–brain barrier. Both [<sup>11</sup>C]<b>7f</b> and [<sup>18</sup>F]<b>7j</b> showed more favorable brain washout pharmacokinetics than [<sup>11</sup>C]<b>8i</b>. In vitro binding assays showed that [<sup>125</sup>I]<b>8i</b> is a very potent α-synuclein radioligand, with K<sub>d</sub> values of 5 nM for both PD brain tissues and LBD-amplified fibrils; it is also selective for PD tissues versus AD or control tissues. These results strongly suggest that the PET probes based on the <i>N</i>-(6-methoxypyridin-3-yl)quinoline-2-amine scaffold have potential utility in detecting α-synuclein aggregates in vivo.
ISSN:2073-4409