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Highly controllable protein self-assembly system with morphological versatility induced by reengineered host-guest interaction

Abstract

Manipulating protein to self-assemble into highly ordered nanostructures not only provide insights into the natural protein assembly process but also allow access to advanced biomaterials. Host-guest interaction has been widely used in the construction of artificial protein assembly in recent years. CB[8] can selectively associate with two tripeptide Phe-Gly-Gly (FGG) tags with an extraordinarily high binding affinity (Kter = 1.5 × 10^11 M^-2). However, the FGG tags utilized before are all fixed to the N-termini via genetic fusion, this spatial limitation greatly confined the availability of CB[8]/FGG pair in the construction of more sophisticated protein nanostructures. Here we first designed and synthesized a maleimide-functionalized Phe-Gly-Gly tag as a versatile site-specific protein modification tool, this designed tag can site-selectively introduce desired guest moities onto protein surfaces for host-guest driven protein assembly. When regulating self-assembly process of protein and CB[8], the constructed protein nanosystem can exhibit distinctive morphological diversity ranging from nanorings, nanospirals, nanowires to superwires. This work developed a new strategy for site-specific protein modification of CB[8] binding tag and provides a possible direction for the construction of ‘smart’, dynamic self-assembly systems.

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Publication details

The article was received on 06 Mar 2017, accepted on 14 May 2017 and first published on 16 May 2017


Article type: Paper
DOI: 10.1039/C7NR01612C
Citation: Nanoscale, 2017, Accepted Manuscript
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    Highly controllable protein self-assembly system with morphological versatility induced by reengineered host-guest interaction

    X. Li, Y. Bai, Z. Huang, C. Si, Z. Dong, Q. Luo and J. Liu, Nanoscale, 2017, Accepted Manuscript , DOI: 10.1039/C7NR01612C

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