Journal
NANOSCALE
Volume 9, Issue 33, Pages 11987-11993Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7nr04370h
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Funding
- NSFC [51403105, 31670973]
- CAMS Initiative for Innovative Medicine [2016-I2M-3-022]
- Science & Technology Projects of Tianjin of China [15JCZDJC38100, 15JCQNJC14300]
- National Program for Support of Top-notch Young Professionals
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The alpha-helix is the most prevalent conformation in proteins. However, formation of the alpha-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 alpha-helical conformation, while a heating-cooling process leads to a conformation more similar to a beta-sheet. The same peptide with different conformations self-assembled into different nanostructures. The peptide with alpha-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 alpha-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 beta-sheet peptide. Our study demonstrates the unique advantages of EISA to assist peptide folding and self-assembly into biofunctional nanomaterials.
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