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Issue 33, 2017
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Enzyme-assisted peptide folding, assembly and anti-cancer properties

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The α-helix is the most prevalent conformation in proteins. However, formation of the α-helical conformation remains a challenge for short peptides with less than 5 amino acids. We demonstrated in this study that enzyme-instructed self-assembly (EISA) provides a unique pathway to assist the self-assembly of peptides into the α-helical conformation, while a heating–cooling process leads to a conformation more similar to a β-sheet. The same peptide with different conformations self-assembled into different nanostructures. The peptide with α-helical conformation self-assembled into stable nanofibers and hydrogels, while the other one assembled into an unstable nanoparticle suspension. The nanofiber solution exhibited better stability against proteinase K digestion and an enhanced cellular uptake compared to the nanoparticle solution. Therefore, the nanomedicine formed by the α-helical peptide showed a better inhibition capacity against cancer cells in vitro and significantly inhibited tumor growth in vivo compared to the one formed by the β-sheet peptide. Our study demonstrates the unique advantages of EISA to assist peptide folding and self-assembly into biofunctional nanomaterials.

Graphical abstract: Enzyme-assisted peptide folding, assembly and anti-cancer properties

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Supplementary files

Article information

18 Jun 2017
27 Jul 2017
First published
09 Aug 2017

Nanoscale, 2017,9, 11987-11993
Article type

Enzyme-assisted peptide folding, assembly and anti-cancer properties

C. Liang, D. Zheng, F. Shi, T. Xu, C. Yang, J. Liu, L. Wang and Z. Yang, Nanoscale, 2017, 9, 11987
DOI: 10.1039/C7NR04370H

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