ABSTRACT

The α/β structural transformation is strongly associated with aggregation of peptides and proteins, some of which are implicated in the neurodegenerative diseases. Our recent research has been addressing such problems by applying some proteins (ovalbumin, α-synuclein) and their homologous peptide fragments (peptide fragments of trichosanthin, reactive center loops of serpins, NAC fragment of synuclein, amyloid peptides). The observations show that the amino-acid sequence of a protein governs its behavior of structural formation and transformation, and the β-sheet-dominant peptide or protein readily aggregates into amyloid-like fibrils.