Amyloid fibrils in superstructures – local ordering revealed by polarization analysis of two-photon excited autofluorescence

Abstract

Protein misfolding products – amyloids – tend to form distinct fibrillar structures of characteristic fold for a given neurodegenerative disease or pathology. Moreover, amyloids (also in intermediate or distorted state)...

Aggregation of gold nanoclusters in amyloid fibers: a luminescence assay for amyloid fibrillation detection and inhibitor screening

“…Protein misfolding and aggregation, that is, amyloid fibrillation, has been proved to be a large factor in such diseases. [1][2][3] Therefore, a new detection method must be established for the process of protein amyloid fibrosis to explore the pathogenesis of these degenerative diseases and screen for the inhibitors of protein fibrosis. [4][5][6][7] Egg white lysozyme is most commonly used in the study of protein fibrosis due to its low price, easy fibrosis, and similarity to the human lysozyme structure.…”

Amyloid engineering – how terminal capping modifies morphology and secondary structure of supramolecular peptide aggregates

“…In all living forms peptides and proteins composed of amino acids give rise to multiple functions regulating the chemistry of life. 1 When the amino acids are arranged in a specific sequence, they can result in structures enabling biological catalysis, [2][3][4] fluorescence, [5][6][7] self-assembly, [8][9][10][11] and many other properties. The self-assembly process of peptides or proteins into amyloid fibrils constitutes an intriguing case.…”

Crown Ether-Capped Gold Nanoclusters as a Multimodal Platform for Bioimaging

“…They exhibit high morphological polymorphism governing their toxicity. , Moreover, self-assembly of amyloidogenic peptides and proteins can lead to the formation of superstructures, namely, spherulites, which are heterogeneous at nano- and microscales. , Spherulites are densely packed spherical superstructures with diameters varying from 5 to 150 μm and composed of unstructured cores and radially growing fibrils . They are characterized by the presence of numerous intermediate states of amyloid aggregates, including mature fibrils . Numerous studies indicated that distinct amyloid fibril morphologies may be more pathogenic than others. , Therefore, rapid structural characterization of amyloids is clinically relevant for diagnosis, classification, and, in further perspective, the treatment of amyloid diseases.…”

“… 41 They are characterized by the presence of numerous intermediate states of amyloid aggregates, including mature fibrils. 42 Numerous studies indicated that distinct amyloid fibril morphologies may be more pathogenic than others. 38 , 43 Therefore, rapid structural characterization of amyloids is clinically relevant for diagnosis, classification, and, in further perspective, the treatment of amyloid diseases.…”