Skip to main content
. 2023 Aug 23;24(17):13110. doi: 10.3390/ijms241713110

Figure 3.

Figure 3

Design of peptide inhibitors based on the core sequence of Aβ fibrosis and their effect on Aβ aggregation. (a) The morphology of AuNCs-CLVFFA through TEM. (b,c) The effect of AuNCs-CLVFFA on Aβ aggregation through ThT and TEM experiments. (d) The effect of IIGL based-peptide on Aβ aggregation induced cytotoxicity through MTT assay. (e) Representation of ABSM 1 illustrating the upper β-strand (recognition β-strand), the δ-linked ornithine turn unit, and the Hao amino acid blocker unit. (f) Schematic diagram of ABSM 1 recognizing and blocking Aβ aggregation through β-sheet interactions. (g) Amino acid sequences from Aβ for the design of ABSMs 1a–g. (h,i) The effect of ABSM 1a on Aβ40 and Aβ42 aggregation monitored using ThT fluorescence and TEM assays. (j) The effect of ABSM 1a on Aβ40 and Aβ42 induced toxicity towards PC-12 cells. (a–c) Reprinted with permission from [63], Copyright 2019, American Chemical Society. (d) Reprinted with permission from [77], Copyright 2004, Elsevier Inc. (Amsterdam, The Netherlands). All rights reserved. (e,h–j) Reprinted with permission from [79], Copyright 2012, Springer Nature Limited (Berlin/Heidelberg, Germany).