Abstract
We demonstrate here that rationally designed block copolypeptides based on poly(L-arginine) and β-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, β-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. Block copolypeptides based on poly(L-arginine) and β-sheet peptide, can form toroidal nanostructures in aqueous solution by rolling-up of 1D nanoribbon and end-to-end connection of the nanoribbon under charge balanced condition. This finding offer new opportunity not only for fabricating more sophisticated peptide-based nanobiomaterials, but for understanding protein misfolding mechanism also.
| Original language | English |
|---|---|
| Pages (from-to) | 191-196 |
| Number of pages | 6 |
| Journal | Macromolecular Rapid Communications |
| Volume | 32 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2011 Jan 17 |
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All Science Journal Classification (ASJC) codes
- Organic Chemistry
- Polymers and Plastics
- Materials Chemistry
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Toroidal nanostructures from self-assembly of block copolypeptides based on poly(L -arginine) and β-sheet peptide. / Lim, Yong-beom; Lee, Eunji; Lee, Myongsoo.
In: Macromolecular Rapid Communications, Vol. 32, No. 2, 17.01.2011, p. 191-196.Research output: Contribution to journal › Article
TY - JOUR
T1 - Toroidal nanostructures from self-assembly of block copolypeptides based on poly(L -arginine) and β-sheet peptide
AU - Lim, Yong-beom
AU - Lee, Eunji
AU - Lee, Myongsoo
PY - 2011/1/17
Y1 - 2011/1/17
N2 - We demonstrate here that rationally designed block copolypeptides based on poly(L-arginine) and β-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, β-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. Block copolypeptides based on poly(L-arginine) and β-sheet peptide, can form toroidal nanostructures in aqueous solution by rolling-up of 1D nanoribbon and end-to-end connection of the nanoribbon under charge balanced condition. This finding offer new opportunity not only for fabricating more sophisticated peptide-based nanobiomaterials, but for understanding protein misfolding mechanism also.
AB - We demonstrate here that rationally designed block copolypeptides based on poly(L-arginine) and β-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, β-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. Block copolypeptides based on poly(L-arginine) and β-sheet peptide, can form toroidal nanostructures in aqueous solution by rolling-up of 1D nanoribbon and end-to-end connection of the nanoribbon under charge balanced condition. This finding offer new opportunity not only for fabricating more sophisticated peptide-based nanobiomaterials, but for understanding protein misfolding mechanism also.
UR - http://www.scopus.com/inward/record.url?scp=78651454764&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78651454764&partnerID=8YFLogxK
U2 - 10.1002/marc.201000512
DO - 10.1002/marc.201000512
M3 - Article
C2 - 21433139
AN - SCOPUS:78651454764
VL - 32
SP - 191
EP - 196
JO - Macromolecular Rapid Communications
JF - Macromolecular Rapid Communications
SN - 1022-1336
IS - 2
ER -