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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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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 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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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. |
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ISSN: | 2050-750X 2050-7518 |
DOI: | 10.1039/d0tb02302g |