Amyloid β (1–42) Folding Multiplicity and Single-Molecule Binding Behavior Studied with STM

Binding Modes of Thioflavin T Molecules to Prion Peptide Assemblies Identified by Using Scanning Tunneling Microscopy

“…This is in analogy to the previous STM observations of the amyloid peptides (β-amyloid 27 and amylin 29 ). The peptides are arranged with their molecular axes approximately perpendicular to the long axis of the lamella.…”

“…The core regions of β-sheet structures have been clearly resolved with STM for the assemblies of amyloid peptides. 27,29 Such progress could also enable the exploration of the interactions between the labeling molecules and peptides. The possibility of visualizing the core ABSTRACT: The widely used method to monitor the aggregation process of amyloid peptide is thioflavin T (ThT) assay, while the detailed molecular mechanism is still not clear.…”

Beta structure motifs of islet amyloid polypeptides identified through surface-mediated assemblies

“…The advances in analytical techniques to resolve the core regions of the beta-sheet and the folding configurations should be of genuine interest in this topical area. Scanning tunneling microscopy (STM) has been applied to study the molecular structures of peptides due to its high structural resolution and adaptability to various environments, especially for amyloid peptides lacking crystalline structures (25,26).Previous STM results revealed amyloid peptide assemblies at liquid-solid interfaces (25-28). An average of 11 amino acid residues have been identified for the core regions of hIAPP (26), which roughly agrees with the model proposed by Luca et al (16).…”

“…The advances in analytical techniques to resolve the core regions of the beta-sheet and the folding configurations should be of genuine interest in this topical area. Scanning tunneling microscopy (STM) has been applied to study the molecular structures of peptides due to its high structural resolution and adaptability to various environments, especially for amyloid peptides lacking crystalline structures (25,26).…”

“…Recent XRD studies have revealed a structural motif of short segments derived from a variety of amyloidal proteins (13)(14)(15). The atomic level structural model for hIAPP [21][22][23][24][25][26][27] revealed a pronounced bend facilitated by Gly 24 , and the model of hIAPP based on the crystalline structures of hIAPP [21][22][23][24][25][26][27] and hIAPP [28][29][30][31][32][33] segments indicated the beta-spine steric zipper structure for hIAPP [23][24][25][26][27][28][29][30][31][32][33][34][35][36][37] (two beta-sheets with interdigitated side chains) (15). The beta-hairpin structure of hIAPP has also been obtained by solid-state nuclear magnetic resonance (NMR) (16), suggesting the parallel beta-sheet structures with 10 residues in the core domains.…”