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利用分子伴侣GroEL的天然双环结构自组装成纳米管，可用于生物医药领域。。 文献制备方法简单，表征手段前沿，可以作为蛋白纳米材料方向研究生的参考资料 1. Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent Scientific Reports http://www.nature.com/srep/2014/ ... full/srep05614.html Volume: 4,Article number:5614 DOI: doi:10.1038/srep05614 Published08 July 2014 Protein nanoassemblies possess unique advantage in biomedical applications such as drug delivery, biocatalysis and vaccine development. Despite recent accomplishment in atomic structure data, the underlying molecular mechanism of protein self-assembly remains elusive, where considerable heterogeneity is often involved. Here we use E. coli chaperonin GroEL, a tetradecameric protein with a molecular weight of 805 kDa, to probe its transformation from cage-like oligomers to protein nanofibers. We show that sodium dodecyl sulfate (SDS), a widely-used protein denaturant, at submicellar concentration binds to and causes partial distortion of GroEL apical domain. Subsequently, the GroEL apical domain with altered secondary structural content converts the GroEL oligomers into modular structural units which are observed to self-assemble into cylindrical nanofibers under an agitated incubation in a physiological buffer. Interestingly, through targeted mutagenesis where two cysteine residues are introduced at the entry site of GroEL cage, we found that the formation of GroEL nanoassembly could be modulated depending on the redox condition of incubation. Without the need of chemical engineering, tunable GroEL nanofibers built by controlled-assembly are among the largest nanoscale bioassembly with broad applications.  2. A Tubular Biocontainer: Metal Ion-Induced 1D Assembly of a Molecularly Engineered Chaperonin J. Am. Chem. Soc., 2009, 131 (22), pp 7556–7557 DOI: 10.1021/ja902696q Publication Date (Web): May 12, 2009 http://pubs.acs.org/doi/abs/10.1021/ja902696q GroELSP/MC, prepared by genetic and chemical modifications of group I chaperonin protein GroEL, site-specifically possesses 28 photochromic (spiropyran [SP] and merocyanine [MC]) units in the entrance parts of its cavity. Addition of divalent metal ions such as Mg2+ to a tris-HCl buffer solution of GroELSP/MC results in one-dimensional (1D) assembly of GroELSP/MC, affording cylindrical hollow fibers with a very large aspect ratio; the longest fiber was 2.5 μm long, corresponding to a 170-mer of GroELSP/MC (MW ≈ 1.4 × 108). When such long fibers are mixed with EDTA, they are cut into short-chain oligomers and eventually into monomeric GroELSP/MC. Similar to GroEL, GroELSP/MC possesses a large binding affinity toward denatured proteins. When GroELSP/MC undergoes 1D assembly after incubation with a denatured protein, guest-containing cylindrical fibers result.  |
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2014-07-30 23:44:53, 6.2 M
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4楼2014-08-03 03:04:25
简单回复
2014-08-02 02:16
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五星好评 顶一下，感谢分享！
2014-08-03 01:29
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五星好评 顶
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五星好评 顶一下，感谢分享！
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三星好评 顶一下，感谢分享！
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2014-10-01 21:48
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五星好评 顶一下，感谢分享！
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