Imaging Flow Cytometry Illuminates New Dimensions of Amyloid Peptide-Membrane Interactions.

摘要: Membrane interactions of amyloidogenic proteins constitute central determinants both in protein aggregation as well amyloid cytotoxicity. Most reported studies peptide-membrane have employed model membrane systems combined with application spectroscopy methods or microscopy analysis individual binding events. Here, we applied for the first time, to our knowledge, imaging flow cytometry investigating representative peptides, namely, 106-126 fragment prion (PrP(106-126)) and human islet polypeptide (hIAPP), giant lipid vesicles. Imaging was also examine inhibition PrP(106-126)-membrane by epigallocatechin gallate, a known modulator peptide aggregation. We show that provided comprehensive population-based statistical information upon morphology changes vesicles induced PrP(106-126) hIAPP. Specifically, experiments reveal hIAPP dramatic transformations vesicles, specifically disruption spherical shapes, reduction vesicle circularity, lobe formation, modulation compactness. Interesting differences, however, were apparent between impact two peptides membranes. The showed gallate ameliorated PrP(106-126). Overall, this study demonstrates provides powerful means disclosing morphological their modulators.