Direct Identification of Amyloid Peptide Fragments in Human α-Synuclein Based on Consecutive Hydrophobic Amino Acids.

ABSTRACT: Formation of amyloid fibrils by misfolding α-synuclein is a characteristic feature of Parkinson's disease, but the exact molecular mechanism of this process has long been an unresolved mystery. Identification of critical amyloid peptide fragments from α-synuclein may hold the key to decipher this mystery. Focusing on consecutive hydrophobic amino acids (CHAA) in the protein sequence, in this study we proposed a sequence-based strategy for direct identification of amyloid peptide fragments in α-synuclein. We picked out three CHAA fragments (two hexapeptides and one tetrapeptide) from α-synuclein and studied their amyloidogenic property. The thioflavin-T binding test, transmission electron microscopy, Congo red staining, and Fourier transform infrared spectroscopy revealed that although only

SUBMITTER: Chen Y 

PROVIDER: S-EPMC7254785 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature