Self-Assembly of Giant Peptide Nanobelts

被引:404
作者
Cui, Honggeng [1 ]
Muraoka, Takahiro [2 ]
Cheetham, Andrew G. [4 ]
Stupp, Samuel I. [1 ,2 ,3 ,4 ]
机构
[1] Northwestern Univ, Dept Mat Sci & Engn, Evanston, IL 60208 USA
[2] Northwestern Univ, Dept Chem, Evanston, IL 60208 USA
[3] Northwestern Univ, Dept Med, Evanston, IL 60208 USA
[4] Northwestern Univ, Inst BioNanotechnol Med, Chicago, IL 60611 USA
基金
美国国家卫生研究院; 美国国家科学基金会;
关键词
NONPOLAR AMINO-ACIDS; SUPRAMOLECULAR ASSEMBLIES; NANOFIBERS; FIBRILS; AMPHIPHILES; MORPHOLOGY; RIBBONS; OLIGOPEPTIDE; CONFORMATION; ARCHITECTURE;
D O I
10.1021/nl802813f
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Many alkylated peptide amphiphiles have been reported to self-assemble into cylindrical nanofibers with diameters on the order of a few nanometers and micrometer scale lengths; these nanostructures can be highly bioactive and are of great Interest in many biomedical applications. We have discovered the sequences for these molecules that can eliminate all curvature from the nanostructures they form In water and generate completely flat nanobelts with giant dimensions relative to previously reported systems. The nanobelts have fairly monodisperse widths on the order of 150 nm and lengths of up to 0.1 mm. The sequences have an alternating sequence with hydrophobic and hydrophilic side chains and variations in monomer concentration generate a "broom" morphology with twisted ribbons that reveals the mechanism through which giant nanobelts form. Interestingly, a variation in pH generates reversibly periodic 2 nm grooves on the surfaces of the nanobelts. With proper functionalization, these nanostructures offer a novel architecture to present epitopes to cells for therapeutic applications.
引用
收藏
页码:945 / 951
页数:7
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