Small molecule fluorescent probes for the detection of amyloid self-assembly in vitro and in vivo

BERTONCINI CW; CELEJ MS

BENTHAM SCIENCE PUBL LTD

Año: 2011 vol. 12 p. 205 - 205

The misfolding and aggregation of amyloidogenic polypeptides are characteristics of many neurodegenerative syndromes including Alzheimer?s and Parkinson?s disease. There is a major interest in the availability of amyloid-specific probes that exhibit fluorescence properties for its use as reporters of protein aggregation in spectroscopy and microscopy methodologies. In this review we intend to provide an overview of novel fluorescence-based probes and procedures appliedfor addressing fundamental aspects of amyloid self-assembly in vitro and in vivo. We highlight the utilization in vitro of several small-molecule fluorescent probes as extrinsic and site-specific reporters of amyloid formation, including single-molecule determinations. Detection of amyloid self-assembly employing compounds such as JC-1, DCVJ, ANS derivatives and luminescent conjugated polymers, as well as site-specific probes such as pyrene and ESIPT is discussed. Wefurther review novel fluorescent pro