Structural characterization of alpha-lactalbumin nanotubes
Nanotubes are formed by self-assembly of the milk protein alpha-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 alpha-lactalbumin nanotube is a heterogeneous self-assembled structure comprising diverse hydrolysis products of alpha-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 alpha-lactalbumin nanotube is proposed to comprise dimeric building blocks, which self-assemble into a 10-start right-handed helix via beta-sheet stacking. The self-assembled protein nanotubes presented here can serve as a model for artificial nanotubes or possibly be used in nanotechnological applications.
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Graveland-Bikker, J.F, Koning, R.I, Koerten, H.K, Geels, R.B.J, Heeren, R.M.A, & de Kruif, C.G. (2009). Structural characterization of alpha-lactalbumin nanotubes. Soft Matter, 5, 2020–2026. doi:10.1039/b815775h