Asymmetric Peptide Nanoribbons

Asymmetry in chemical structure or shape at molecular, nanoscale, or microscopic levels is essential to a vast number of functionalities in both natural and artificial systems. Bottom-up approaches to create asymmetric supramolecular nanostructures are considered promising but this strategy suffers...

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Bibliographic Details
Published in:	Nano letters 2016-10, Vol.16 (11)
Main Authors:	Yu, Zhilin, Tantakitti, Faifan, Palmer, Liam C., Stupp, Samuel I.
Format:	Article
Language:	eng
Subjects:	Asymmetric nanostructures GENERAL AND MISCELLANEOUS INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY monomers multidomain peptide amphiphiles nanoparticles nanoribbons NANOSCIENCE AND NANOTECHNOLOGY Nanostructures, Peptides and proteins, Monomers, Nanoparticles, Noncovalent interactions noncovalent interactions peptides and proteins supramolecular self-assembly
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Summary:	Asymmetry in chemical structure or shape at molecular, nanoscale, or microscopic levels is essential to a vast number of functionalities in both natural and artificial systems. Bottom-up approaches to create asymmetric supramolecular nanostructures are considered promising but this strategy suffers from the potentially dynamic nature of noncovalent interactions. We report here on supramolecular self-assembly of asymmetric peptide amphiphiles consisting of two different molecularly linked domains. We found that strong noncovalent interactions and a high degree of internal order among the asymmetric amphiphiles lead to nanoribbons with asymmetric faces due to the preferential self-association of the two domains. The capture of gold nanoparticles on only one face of the nanoribbons demonstrates symmetry breaking in these supramolecular structures.
ISSN:	1530-6984 1530-6992