Peptide self-assembly triggered by metal ions

被引:247
作者
Zou, Rongfeng [1 ,2 ]
Wang, Qi [3 ]
Wu, Junchen [1 ,2 ]
Wu, Jingxian [1 ,2 ]
Schmuck, Carsten [4 ]
Tian, He [1 ,2 ]
机构
[1] E China Univ Sci & Technol, Key Lab Adv Mat, Shanghai 200237, Peoples R China
[2] E China Univ Sci & Technol, Inst Fine Chem, Shanghai 200237, Peoples R China
[3] Nantong Univ, Coll Publ Hlth, Nantong 226019, Peoples R China
[4] Univ Duisburg Essen, Inst Organ Chem, D-45117 Essen, Germany
基金
中国国家自然科学基金;
关键词
HUMAN CARBONIC-ANHYDRASE; HISTIDINE-TAGGED PROTEINS; COLLAGEN PEPTIDES; AMYLOID FORMATION; AMINO-ACIDS; AFFINITY-CHROMATOGRAPHY; INTERMOLECULAR FORCES; BINDING; COORDINATION; DESIGN;
D O I
10.1039/c5cs00234f
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Through their unique and specific interactions with various metal ions, naturally occurring proteins control structures and functions of many biological processes and functions in organisms. Inspired by natural metallopeptides, chemists have developed artificial peptides which coordinate with metal ions through their functional groups either for introducing a special reactivity or for constructing nano-structures. However, the design of new coordination peptides requires a deep understanding of the structures, assembly properties, and dynamic behaviours of such peptides. This review briefly discusses strategies of peptide self-assembly induced by metal coordination to different natural and non-natural binding sites in the peptide. The structures and functions of the obtained aggregates are described as well. We also highlight some examples of a metal-induced peptide self-assembly with relevance to biotechnology applications.
引用
收藏
页码:5200 / 5219
页数:20
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