SCHEDULED MAINTENANCE
Synthesis and characterization of high affinity fluorogenic α-synuclein probes†
Zsofia
Lengyel-Zhand, 
‡a
John J.
Ferrie,
‡b
Bieneke
Janssen,
a
Conor M.
Haney,
§b
E. James
Petersson
*b
and
Robert H.
Mach
*a
‡a
John J.
Ferrie,
‡b
Bieneke
Janssen,
a
Conor M.
Haney,
§b
E. James
Petersson
*b
and
Robert H.
Mach
*a
Abstract
Fluorescent small molecules are powerful tools for imaging α-synuclein pathology in vitro and in vivo. In this work, we explore benzofuranone as a potential scaffold for the design of fluorescent α-synuclein probes. These compounds have high affinity for α-synuclein, show fluorescent turn-on upon binding to fibrils, and display different binding to Lewy bodies, Lewy neurites and glial cytoplasmic inclusion pathologies in post-mortem brain tissue. These studies not only reveal the potential of benzofuranone compounds as α-synuclein specific fluorescent probes, but also have implications for the ways in which α-synucleinopathies are conformationally different and display distinct small molecule binding sites.
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