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【奖励】本帖被评价6次，作者rockyss增加金币 4.2 个

rockyss

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[资源] 【推荐】 JACS和scientific report报道-可控自组装蛋白纳米管

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.