Figure 1 | Scientific Reports

Figure 1

From: A rationally designed bicyclic peptide remodels Aβ42 aggregation in vitro and reduces its toxicity in a worm model of Alzheimer’s disease

Figure 1

Sequence and synthesis of DesBP, the rationally designed bicyclic peptide described in this work. (a) A 23-residue sequence was rationally designed to bind the C-terminal region (residues 31–42) of Aβ42 through two binding regions (green arrows); three cysteine residues were inserted for cyclization (orange) and six positively charged residues (blue) were added outside the binding regions to improve the solubility of the designed sequence for the bicyclic peptide (DesBP). (b) Representation of the designed binding mode of DesBP. Dotted lines mark residues predicted to be involved in backbone-backbone hydrogen bonding and arrows denote the N- to C-terminus direction. (c) Synthesis of DesBP. The rationally-designed 23-residue peptide was tethered through its three cysteine residues to the trifunctional compound 1,3,5-tris(bromomethyl)benzene (TBMB) in a nucleophilic substitution reaction (see “Materials and methods” section).

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