In discussing the use of AMPP to affect β-hairpin formation peptides, we inadvertently failed to appropriately acknowledge the previous use of AMPP in amyloid-like peptides. As discussed in ref 33 (Deeg, A. A., et al. (2011) ChemPhysChem12, 559–562), Zinth et al. have demonstrated that AMPP influences the assembly and disassembly of amyloid-like structures by the Ac-SWTWE-AMPP-KWTWK-NH2 (ac-AzoTrpZip2) peptide through cis–trans isomerization. Ac-AzoTrpZip2 also assembles in the trans conformation, and the resulting fibrils apparently disassemble upon trans to cis isomerization. Our data are in good agreement with this precedent as trans-2 and trans-3 Aβ peptides self-assemble into amyloid fibrils similar to wild-type Aβ, whereas cis-2 and cis-3 instead form amorphous aggregates; trans–cis isomerization of fibrils also perturbs fibril populations in our systems.
Reference 35 should be corrected to Dong, S.-L., Löweneck, M., Schrader, T. E., Schreier, W. J., Zinth, W., Moroder, L., and Renner, C. (2006) A Photocontrolled β-Hairpin Peptide. Chem.—Eur. J.12, 1114–1120.