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- W2007236469 abstract "Amyloid fibril formation is assumed to be the molecular basis for a variety of diseases of unrelated origin. Despite its fundamental clinical importance, the mechanism of amyloid formation is not fully understood. When we analyzed a variety of short functional fragments from unrelated amyloid-forming proteins, a remarkable occurrence of aromatic residues was observed. The finding of aromatic residues in diverse fragments raises the possibility that pi-pi interactions may play a significant role in the molecular recognition and self-assembly processes that lead to amyloid formation. This is in line with the well-known central role of pi-stacking interactions in self-assembly processes in the fields of chemistry and biochemistry. We speculate that the stacking interactions may provide energetic contribution as well as order and directionality in the self-assembly of amyloid structures. Experimental data regarding amyloid formation and inhibition by short peptide analogs also support our hypothesis. The pi-stacking hypothesis suggests a new approach to understanding the self-assembly mechanism that governs amyloid formation and indicates possible ways to control this process." @default.
- W2007236469 created "2016-06-24" @default.
- W2007236469 creator A5082716768 @default.
- W2007236469 date "2002-01-01" @default.
- W2007236469 modified "2023-10-16" @default.
- W2007236469 title "A possible role for π‐stacking in the self‐assembly of amyloid fibrils" @default.
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- W2007236469 doi "https://doi.org/10.1096/fj.01-0442hyp" @default.
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