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Enhanced Fluorescent Assignment of Protein Aggregates by an Oligothiophene–Porphyrin‐Based Amyloid Ligand
Author(s) -
Arja Katriann,
Sjölander Daniel,
Åslund Alma,
Prokop Stefan,
Heppner Frank L.,
Konradsson Peter,
Lindgren Mikael,
Hammarström Per,
Åslund K. O. Andreas,
Nilsson K. Peter R.
Publication year - 2013
Publication title -
macromolecular rapid communications
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.348
H-Index - 154
eISSN - 1521-3927
pISSN - 1022-1336
DOI - 10.1002/marc.201200817
Subject(s) - porphyrin , fluorescence , amyloid (mycology) , ligand (biochemistry) , chemistry , biophysics , protein aggregation , photochemistry , biochemistry , biology , receptor , inorganic chemistry , physics , quantum mechanics
Fluorescent probes identifying protein aggregates are of great interest, as deposition of aggregated proteins is associated with many devastating diseases. Here, we report that a fluorescent amyloid ligand composed of two distinct molecular moieties, an amyloidophilic pentameric oligothiophene and a porphyrin, can be utilized for spectral and lifetime imaging assessment of recombinant Aβ 1‐42 amyloid fibrils and Aβ deposits in brain tissue sections from a transgenic mouse model with Alzheimer's disease pathology. The enhanced spectral range and distinct lifetime diversity of this novel oligothiophene–porphyrin‐based ligand allow a more precise assessment of heterogeneous amyloid morphology compared with the corresponding oligothiophene dye.