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Therése Klingstedt, Dr. Hamid Shirani, Dr. K. O. Andreas Åslund, Dr. Nigel J. Cairns, Dr. Christina J. Sigurdson, Prof. Michel Goedert and Dr. K. Peter R. Nilsson The Structural Basis for Optimal Performance of Oligothiophene-Based Fluorescent Amyloid Ligands: Conformational Flexibility is Essential for Spectral Assignment of a Diversity of Protein Aggregates Chemistry - A European Journal 19

Article first published online: 18 JUN 2013 | DOI: 10.1002/chem.201301463

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Freedom! Conformational freedom and extended conjugation of the conjugated backbone are important determinants for thiophene-based optical ligands for spectral assignment of disease-associated protein aggregates. Replacing the central thiophene ring with a phenyl moiety (see figure) abolished the spectral assignment of Aβ and tau aggregates as well as the detection of non-congophilic and non-thioflavinophilic protein aggregates.

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