Rational Design of a Tetrameric Protein to Enhance Interactions between Self-Assembled Fibers Gives Molecular Hydrogels

被引:116
作者
Zhang, Xiaoli [1 ,2 ]
Chu, Xinlei [1 ,2 ]
Wang, Ling [3 ,4 ]
Wang, Huaimin [1 ,2 ]
Liang, Gaolin [5 ]
Zhang, Jinxiu [1 ,2 ]
Long, Jiafu [1 ,2 ]
Yang, Zhimou [1 ,2 ]
机构
[1] Nankai Univ, State Key Lab Med Chem Biol, Tianjin 300071, Peoples R China
[2] Nankai Univ, Coll Life Sci, Tianjin 300071, Peoples R China
[3] Nankai Univ, Coll Pharm, Tianjin 300071, Peoples R China
[4] Nankai Univ, Tianjin Key Lab Mol Drug Res, Tianjin 300071, Peoples R China
[5] Univ Sci & Technol China, Dept Chem, CAS Key Lab Soft Matter Chem, Hefei 230026, Anhui, Peoples R China
关键词
hydrogels; mechanical properties; protein-peptide interactions; proteins; self-assembly; PEPTIDE HYDROGEL; DRUG-DELIVERY; SUPRAMOLECULAR GELS; PHYSICAL HYDROGELS; ENCAPSULATION; PRODRUGS; GROWTH;
D O I
10.1002/anie.201108612
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Styling gels: The fusion protein ULD-TIP-1 (ULD=ubiquitin-like domain, TIP-1=Tax-interacting protein-1) enhances the interactions between self-assembled fibers formed by small molecules bearing a peptide that specifically binds to the ULD-TIP-1. The mechanical properties of the resulting hydrogels (see picture) are tuned by using peptides with different dissociation constants for the protein. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:4388 / 4392
页数:5
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