Structural characterization of alpha-lactalbumin nanotubes PDF Print E-mail

J.F. Graveland-Bikker, R.I. Koning, H.K. Koerten, R.B.J. Geels, R.M.A. Heeren, C.G. de Kruif

Soft Matter, 2009, 5, 2020-2026 

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.

http://dx.doi.org/10.1039/b815775h 

 
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