Engineering Amyloid Fibrils from β-Solenoid Proteins for Biomaterials Applications

被引：51

作者：

Peralta, Maria D. R. ^{[1
]}

Karsai, Arpad ^{[1
]}

Ngo, Alice ^{[1
]}

Sierra, Catherine ^{[1
]}

Fong, Kai T. ^{[1
]}

Hayre, Natha Robert ^{[2
,3
]}

Mirzaee, Nima ^{[2
,3
]}

Ravikumar, Krishnakumar Mayuram ^{[2
,3
]}

Kluber, Alexander J. ^{[3
,4
]}

Chen, Xi ^{[1
]}

Liu, Gang-yu ^{[1
]}

Toney, Michael D. ^{[1
]}

Singh, Rajiv. R. ^{[2
,3
]}

Cox, Daniel Lee ^{[2
,3
]}

机构：

[1] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA

[2] Univ Calif Davis, Dept Phys, Davis, CA 95616 USA

[3] Univ Calif Davis, Inst Complex Adapt Matter, Davis, CA 95616 USA

[4] Rice Univ, Dept Chem, Houston, TX 77251 USA

来源：

ACS NANO | 2015年 / 9卷 / 01期

基金：

美国国家科学基金会;

关键词：

amyloid; antifreeze protein; beta-solenoid; atomic force microscopy; thioflavin-T fluorescence; PENTAPEPTIDE REPEAT PROTEIN; CIRCULAR-DICHROISM SPECTRA; THIOFLAVIN-T-BINDING; ANTIFREEZE PROTEIN; SECONDARY STRUCTURE; CRYSTAL-STRUCTURE; SPIDER SILK; AGGREGATION; NANOWIRES; PEPTIDES;

D O I：

10.1021/nn5056089

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Nature provides numerous examples of self-assembly that can potentially be implemented for materials applications. Considerable attention has been given to one-dimensional cross-beta or amyloid structures that can serve as templates for wire growth or strengthen materials such as glue or cement. Here, we demonstrate controlled amyloid self-assembly based on modifications of beta-solenoid proteins. They occur naturally in several contexts (e.g., antifreeze proteins, drug resistance proteins) but do not aggregate in vivo due to capping structures or distortions at their ends. Removal of these capping structures and regularization of the ends of the spruce budworm and rye grass antifreeze proteins yield micron length amyloid fibrils with predictable heights, which can be a platform for biomaterial-based self-assembly. The design process, including all-atom molecular dynamics simulations, purification, and self-assembly procedures are described. Fibril formation with the predicted characteristics is supported by evidence from thioflavin-T fluorescence, circular dichroism, dynamic light scattering, and atomic force microscopy. Additionally, we find evidence for lateral assembly of the modified spruce budworm antifreeze fibrils with sufficient incubation time. The kinetics of polymerization are consistent with those for other amyloid formation reactions and are relatively fast due to the preformed nature of the polymerization nucleus.

引用

页码：449 / 463

页数：15

共 73 条

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