CROSS-DISCIPLINARY PHYSICS AND RELATED AREAS OF SCIENCE AND TECHNOLOGY |
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Photo-Crosslinking Induced Geometric Restriction Controls the Self-Assembly of Diphenylalanine Based Peptides |
TIE Zuo-Xiu, QIN Meng**, ZOU Da-Wei, CAO Yi**, WANG Wei
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National Laboratory of Solid State Microstructure and Department of Physics, Nanjing University, Nanjing 210093
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Cite this article: |
TIE Zuo-Xiu, QIN Meng, ZOU Da-Wei et al 2011 Chin. Phys. Lett. 28 028702 |
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Abstract The diphenylalanine (FF) motif has been widely used in the design of peptides that are capable of forming various ordered structures, such as nanotubes, nanospheres and hydrogels. In these assemblies, FF based peptides adopt an antiparallel structure and are stabilized by π−π stacking among the phenyl groups. Here we show that assembly of FF-based peptides can be controlled by their geometric restrictions. Using tripeptide FFY (L-Phe-L-Phe-L-Tyr) as an example, we demonstrate that photo-crosslinking of C-terminal tyrosine can impose a geometric restriction to the formation of an antiparallel structure, leading to a structural change of the assemblies from nanosphere to amorphous. This finding is confirmed using far-UV circular dichroism, Fourier transform infrared spectroscopy and atomic force microscopy. Based on such a mechanism, we are able to control the gel-sol transition of Fmoc-FFY using the geometric restriction induced by photo-crosslinking of C-terminal tyrosine groups. We believe that geometric restriction should be considered as an important factor in the design of peptide-based materials. It can also be implemented as a useful strategy for the construction of environment-responsive "smart" materials.
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Keywords:
87.85.Jf
87.85.Jc
87.15.-v
64.75.Yz
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Received: 01 November 2010
Published: 30 January 2011
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PACS: |
87.85.jf
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(Bio-based materials)
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87.85.jc
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(Electrical, thermal, and mechanical properties of biological matter)
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87.15.-v
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(Biomolecules: structure and physical properties)
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64.75.Yz
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(Self-assembly)
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