Structural insights into peptide self-assembly using photo-induced crosslinking experiments and discontinuous molecular dynamics.

ABSTRACT: Determining the structure of the (oligomeric) intermediates that form during the self-assembly of amyloidogenic peptides is challenging because of their heterogeneous and dynamic nature. Thus, there is need for methodology to analyze the underlying molecular structure of these transient species. In this work, a combination of fluorescence quenching, photo-induced crosslinking (PIC) and molecular dynamics simulation was used to study the assembly of a synthetic amyloid-forming peptide, Aβ_16-22. A PIC amino acid containing a trifluormethyldiazirine (TFMD) group-Fmoc(TFMD)Phe-was incorporated into the sequence (Aβ*_16-22). Electrospray ionization ion-mobility spectrometry mass-spectrometry (ESI-IMS-MS) analysis of the PIC products confirmed that Aβ*_16-22 forms

SUBMITTER: Bunce SJ 

PROVIDER: S-EPMC7988534 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature