Intrinsic blue-green fluorescence in amyloyd fibrils

Abstract

Proteins and polypeptides containing a high proportion of β-sheets have been recently reported to exhibit, in their amyloid aggregated states, an intrinsic fluorescence in the blue-green range of wavelength where the aromatic residues do not emit. Lately, growing attention has been devoted to the identification of a specific, structure-related fluorophore for the detection of amyloid aggregates due to their implications in the physio-pathology of neurodegenerative diseases and other aggregation-related diseases. Indeed, the appearance of blue-green fluorescence could be used as an alternative method for the investigation and the detection of the aggregation state without using external probes. Several hypotheses have been suggested to explain the molecular bases of this rather unusual intrinsic emission. In particular, it has been related to an expansion of the electronic delocalization of π-electrons of peptide bonds through the backbone-to-backbone hydrogen bonds connecting the β-sheets. Alternatively, the formation of the intrinsic chromophore has been associated to chemical modifications of the aromatic residues or arising from dipolar coupling between excited states of aromatic amino acids densely packed in the fibril structures. More recently, it has been proposed that the blue-green amyloid fluorophore does not require neither the presence of aromatic residues nor multiple bond conjugation. In this study, we critically review the above hypotheses with particular attention to the electronic transitions responsible for the appearance of blue-green fluorescence in amyloid fibrils.

Keywords

• amyloid aggregation
• amyloid fibrils
• cross-β structure
• intrinsic blue-green fluorescence