Fig. 1: Characterizations of aggregates of pathogenic (Aβ, αS, IAPP) and functional (FapC) amyloid proteins.
From: Endothelial leakiness elicited by amyloid protein aggregation
a Amino acid sequences of the four amyloid proteins used in the study. Red: negative charge, dark cyan: hydrophobic, blue: positive charge, orange: polar uncharged amino acids, and gray: special cases. b–e Transmission electron microscopy imaging of different amyloid protein species: b Aβ, c αS, d IAPP, and e FapC (n = 3 biologically independent samples). The label “m” stands for monomers, “o” for oligomers, “o-p” for early-stage protofibrils transitioning from the oligomers, “f” for fibrils, and “s” for sonicated seeds, respectively. f ThT kinetic assay of amyloid protein fibrillization. Data are expressed as mean ± SD (n = 3 biologically independent samples). g Lengths of different amyloid protein aggregates based on TEM imaging. Data are expressed as mean ± SD (n = 17, 71, 24, 4, 16, 13, 15, 13, 14, 7, 15, 4, 15 and 24 protein aggregates of Aβm, Aβo, Aβo-p, Aβf, Aβs, αSm, αSo, αSf, αSs, IAPPm, IAPPo, IAPPf, IAPPs, and FapCs, respectively, examined over three independent samples).
