Inhibition of peptide amyloid formation by cationic peptides with homologous sequences.
We have studied the model peptides that undergo self-initiated structural transition from alpha-helix to beta-sheet and self-assembling into amyloid fibrils. We here constructed an inhibition system of amyloid formation utilizing homologous recognition and assembly of peptides with increased solubility. Among 20 peptides with homologous sequences examined here, cationic peptides showed the stronger inhibition ability against the amyloid formation of a model peptide.
Yamashita
Taro
T
Department of Bioengineering, Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.
Takahashi
Yuta
Y
Takahashi
Tsuyoshi
T
Mihara
Hisakazu
H
D000595:Amino Acid Sequence; D000682:Amyloid / Q000037:antagonists & inhibitors* / Q000737:chemistry*; D002942:Circular Dichroism; D015195:Drug Design; D009842:Oligopeptides / Q000138:chemical synthesis* / Q000494:pharmacology*; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013329:Structure-Activity Relationship
D000682:Amyloid; D009842:Oligopeptides