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PMID: 16608254 Published · ppublish English Evaluation Study Journal Article Research Support, Non-U.S. Gov't

Structural and mechanical study of a self-assembling protein nanotube.

Nano letters ·Vol. 6 ·No. 4 ·2006-04-00 ·Pages 616-21

Graveland-Bikker JF, Schaap IA, Schmidt CF, de Kruif CG

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.

MeSH Terms
Computer Simulation Crystallization/methods Dimerization Elasticity Lactalbumin/chemistry,ultrastructure Materials Testing Mechanics Models, Chemical Multiprotein Complexes/chemistry,ultrastructure Nanotechnology/methods Nanotubes/chemistry,ultrastructure Particle Size Protein Binding Protein Conformation Stress, Mechanical Tensile Strength
Chemicals
Multiprotein Complexes Lactalbumin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Graveland-Bikker J F
NIZO food research, P.O. Box 20, 6710 BA Ede, The Netherlands. joanke@mit.edu
Schaap I A T
Schmidt C F
de Kruif C G
Article Info
Journal
Nano letters
Abbr.
Nano Lett
ISSN
1530-6984
Published
2006-04-00
Pages
616-21
Language
English
Region
United States
NLM ID
101088070
Subset
IM
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