Structural and mechanical study of a self-assembling protein nanotube

J.F. Graveland-Bikker, IAT Schaap, C.F. Schmidt, C.G. de Kruif

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Abstract

We report a structural characterization of self-assembling nanostructures. Using atomic force microscopy (AFM), we discovered that partially hydrolyzed alpha-lactalbumin organizes in a 10-start helix forming tubes with diameters of only 21 nm. We probed the mechanical strength of these nanotubes by locally indenting them with an AFM tip. To extract the material properties of the nanotubes, we modeled the experiment using finite element methods. Our study shows that artificial helical protein self-assembly can yield very stable, strong structures that can function either as a model system for artificial self-assembly or as a nanostructure with potential for practical applications.

Original languageEnglish
Pages (from-to)616-621
Number of pages6
JournalNano Letters
Volume6
Issue number4
DOIs
Publication statusPublished - Apr 2006

Keywords

  • ATOMIC-FORCE MICROSCOPY
  • HYDROLYZED ALPHA-LACTALBUMIN
  • ELASTIC PROPERTIES
  • NANOTECHNOLOGY
  • PEPTIDES
  • DESIGN

Cite this

Graveland-Bikker, J. F., Schaap, IAT., Schmidt, C. F., & de Kruif, C. G. (2006). Structural and mechanical study of a self-assembling protein nanotube. Nano Letters, 6(4), 616-621. https://doi.org/10.1021/nl052205h