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Left-Handed Helical Ribbon Intermediates in the Self-Assembly of a β-Sheet Peptide

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Department of Mechanical Engineering, Center for Biomedical Engineering, and Division of Bioengineering and Environmental Health, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139-4307
Cite this: Nano Letters 2002, 2, 4, 295–299
Publication Date (Web):February 21, 2002
Copyright © 2002 American Chemical Society

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    We report the observation of intermediate structures in the self-assembly of the peptide KFE8 (FKFEFKFE), designed with alternating polar and nonpolar amino acids. Self-assembly was followed over time using atomic force microscopy (AFM), transmission electron microscopy (TEM), and circular dichroism (CD). Molecular dynamics simulations suggest that these intermediates are left-handed double helical β-sheets. These findings have implications in the study of β-sheet fibril formation, and in the molecular design of materials.

     Department of Mechanical Engineering.

     Center for Biomedical Engineering.


     Division of Bioengineering and Environmental Health.


     To whom correspondence should be addressed. E-mail:  shuguang@, [email protected].

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