Amyloid-forming propensity of the hydrophobic non-natural amino acid on the fibril-forming core peptide of human tau.
Amino acid residues with aromatic side chains, such as Tyr and Phe, are known to play essential roles in forming and stabilizing the amyloid fibrils of pathogenic polypeptides by affecting their amyloid forming propensity. We have studied the amyloid-type aggregation of peptides containing non-natural amino acid derived from a core part of human pathogenic protein, tau. The hydrophobic nature of the biphenyl group and its intermolecular aromatic interactions strongly alter their amyloid formation properties.
Hirata
Akiyoshi
A
Institute of Advanced Energy, Kyoto University, Matsuoka, Yoshida, Fukui 910-1193, Japan.
Sugimoto
Kenji
K
Konno
Takashi
T
Morii
Takashi
T
D000596:Amino Acids / Q000737:chemistry*; D024322:Amino Acids, Aromatic / Q000737:chemistry; D000682:Amyloid / Q000737:chemistry* / Q000648:ultrastructure; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D046529:Microscopy, Electron, Transmission; D010455:Peptides / Q000737:chemistry; D012995:Solubility; D016875:tau Proteins / Q000737:chemistry*
D000596:Amino Acids; D024322:Amino Acids, Aromatic; D000682:Amyloid; D010455:Peptides; D016875:tau Proteins