IBR   13079
INSTITUTO DE BIOLOGIA MOLECULAR Y CELULAR DE ROSARIO
Unidad Ejecutora - UE
artículos
Título:
Protein amyloids develop an intrinsic fluorescence signature during aggregation
Autor/es:
FIONA T.S. CHAN; GABRIELE S. KAMINSKI SCHIERLE; JANET R. KUMITA; CARLOS W. BERTONCINI; CHRISTOPHER M. DOBSON; CLEMENS F. KAMINSKI
Revista:
ANALYST
Editorial:
ROYAL SOC CHEMISTRY
Referencias:
Lugar: CAMBRIDGE; Año: 2013 vol. 138 p. 2156 - 2162
ISSN:
0003-2654
Resumen:
We report observations of an intrinsic fluorescence in the visible
range, which develops during the aggregation of a range of polypeptides,
including the disease-related human peptides amyloid-β(140) and
(142), lysozyme and tau. Characteristic fluorescence properties such as
the emission lifetime and spectra were determined experimentally. This
intrinsic fluorescence is independent of the presence of aromatic
side-chain residues within the polypeptide structure. Rather, it appears
to result from electronic levels that become available when the
polypeptide chain folds into a cross-β sheet scaffold similar to what
has been reported to take place in crystals. We use these findings to
quantify protein aggregation in vitro by fluorescence imaging in a label-free manner.