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Self-assembling nitrilotriacetic acid nanofibers for tracking and enriching His-tagged proteins in living cells

Specific and expeditious identification and enrichment of target proteins in living cells is often a challenging task. The hexahistidine (6His) tag is frequently used to label artificially engineered proteins produced in prokaryotic or eukaryotic cells. Utilizing the interaction between 6His-tag and...

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Bibliographic Details
Published in:Journal of materials chemistry. B, Materials for biology and medicine Materials for biology and medicine, 2021-01, Vol.9 (1), p.8-84
Main Authors: Zhang, Li-Song, Yin, Yi-Lun, Wang, Lei, Xia, Ying, Ryu, SungJu, Xi, Zhen, Li, Lu-Yuan, Zhang, Zhi-Song
Format: Article
Language:English
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Summary:Specific and expeditious identification and enrichment of target proteins in living cells is often a challenging task. The hexahistidine (6His) tag is frequently used to label artificially engineered proteins produced in prokaryotic or eukaryotic cells. Utilizing the interaction between 6His-tag and nitrilotriacetic acid (NTA) mediated by divalent metal ions (Ni 2+ , Cu 2+ , Zn 2+ or Co 2+ ), we designed and synthesized a series of Nap-G/Biotin/ANA-FFpYGK-NTA probes that, assisted by alkaline phosphatase (ALP), self-assemble into nanofibers. The probe consists of an NTA group that specifically binds to 6His-tag, an FFpY group that promotes self-assembly facilitated by ALP, and a hydrophobic (Nap-G/ANA/Biotin) capping group for various applications. We demonstrate that the ANA-FFpYGK-NTA(Ni 2+ ) nanofibers are fit for real-time tracking of His-tagged protein in living cells, and the Biotin-FFpYGK-NTA(Ni 2+ ) nanofibers are for isolating His-tagged proteins and other proteins that they interact with. A supramolecular self-assembling nitrilotriacetic acid nanofiber probe for tracking and enriching His-tagged proteins in living cells.
ISSN:2050-750X
2050-7518
DOI:10.1039/d0tb02302g