Journal
MACROMOLECULAR RAPID COMMUNICATIONS
Volume 32, Issue 2, Pages 191-196Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/marc.201000512
Keywords
biomaterials; peptides; self-assembly; beta-sheets; toroids
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Funding
- National Research Foundation (NRF) of Korea
- U.S. Air Force Office of Scientific Research [FA 2386-10-1-4087]
- NRF [2010-0019102]
- Basic Science Research Program [2010-0015374, 2010-0016145]
- Translational Research Center for Protein Function Control, Yonsei University [2010-0001933]
- National Research Foundation of Korea [2009-0082617, 2009-0066736, 2002-0046425, 2009-0092971] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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We demonstrate here that rationally designed block copolypeptides based on poly(L-arginine) and beta-sheet peptides can form toroidal nanostructures. In aqueous solution, we found that 1D nanoribbons roll up and connect in an end-to-end fashion under charge-balanced conditions, resulting in the formation of barrel-like toroidal nanostructures. Toroidal diameter was highly uniform (10 nm), indicating that there is a preferred geometrical packing requirement for toroid formation. Our results demonstrate that, when suitably designed, beta-sheet nanostructures can be manipulated to form more complex 2D nanostructures. This finding offers new opportunities not only for the fabrication of more sophisticated peptide-based nanobiomaterials, but also for understanding and inhibiting protein misfolding diseases.
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