INVESTIGADORES
BERTONCINI Carlos Walter
artículos
Título:
Small molecule fluorescent probes for the detection of amyloid self-assembly in vitro and in vivo
Autor/es:
CARLOS W. BERTONCINI; MARÍA S. CELEJ
Revista:
CURRENT PROTEIN AND PEPTIDE SCIENCE
Editorial:
BENTHAM SCIENCE PUBL LTD
Referencias:
Lugar: Oak Park; Año: 2011 vol. 12 p. 206 - 220
ISSN:
1389-2037
Resumen:
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 applied for 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.
We further review novel fluorescent probes developed for the
non-invasive optical imaging of protein aggregates in vivo, including
BTA-1, Methoxy-X04, NIAD-4 and CRANAD-2. Availability of increasingly
versatile amyloid-specific fluorescent probes is having a very positive
impact in the drug discovery and diagnostics fields.