Structural characterization of α-lactalbumin nanotubes

被引：29

作者：

Graveland-Bikker, Johanna F. ^{[1
]}

Koning, Roman I. ^{[2
]}

Koerten, Henk K. ^{[2
]}

Geels, Rimco B. J. ^{[3
]}

Heeren, Ron M. A. ^{[3
]}

de Kruif, Cornelis G. ^{[1
,4
]}

机构：

[1] NIZO Food Res, NL-6710 BA Ede, Netherlands

[2] Leiden Univ, Med Ctr, Dept Mol Cell Biol, Sect Electron Microscopy, NL-2300 RC Leiden, Netherlands

[3] FOM, Inst Atom & Mol Phys, NL-1098 SJ Amsterdam, Netherlands

[4] Univ Utrecht, Debye Res Inst, Vant Hoff Lab Phys Chem, NL-3584 CH Utrecht, Netherlands

来源：

SOFT MATTER | 2009年 / 5卷 / 10期

关键词：

D O I：

10.1039/b815775h

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

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.

引用

页码：2020 / 2026

页数：7

共 25 条

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