Journal
JOURNAL OF MATERIALS CHEMISTRY B
Volume 9, Issue 1, Pages 80-84Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d0tb02302g
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Funding
- National Natural Science Foundation of China (NSFC) projects [81672740, 81972687, 81874167]
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A Nap-G/Biotin/ANA-FFpYGK-NTA probe has been designed for specific and rapid enrichment of target proteins in living cells by self-assembling into nanofibers, with functionalities like specific binding to 6His-tag and promotion of self-assembly. The probe demonstrates suitability for real-time tracking and isolation of His-tagged proteins.
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 (Ni2+, Cu2+, Zn2+ or Co2+), 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(Ni2+) nanofibers are fit for real-time tracking of His-tagged protein in living cells, and the Biotin-FFpYGK-NTA(Ni2+) nanofibers are for isolating His-tagged proteins and other proteins that they interact with.
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