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Issue 10, 2009
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Structural characterization of α-lactalbumin nanotubes

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Nanotubes are formed by self-assembly of the milk protein α-lactalbumin, after partial hydrolysis by a protease from Bacillus licheniformis. These unique nanotubes are formed only in the presence of an appropriate cation at neutral pH. The α-lactalbumin nanotube is a heterogeneous self-assembled structure comprising diverse hydrolysis products of α-lactalbumin with molar masses around 11 kDa. On the basis of the mass spectrometry, circular dichroism and cryo-electron microscopy results presented here, and previous atomic force microscopy and scattering results, the α-lactalbumin nanotube is proposed to comprise dimeric building blocks, which self-assemble into a 10-start right-handed helix via β-sheet stacking. The self-assembled protein nanotubes presented here can serve as a model for artificial nanotubes or possibly be used in nanotechnological applications.

Graphical abstract: Structural characterization of α-lactalbumin nanotubes

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Article information

09 Sep 2008
26 Jan 2009
First published
30 Mar 2009

Soft Matter, 2009,5, 2020-2026
Article type

Structural characterization of α-lactalbumin nanotubes

J. F. Graveland-Bikker, R. I. Koning, H. K. Koerten, R. B. J. Geels, R. M. A. Heeren and C. G. de Kruif, Soft Matter, 2009, 5, 2020
DOI: 10.1039/B815775H

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