Self-assembling nitrilotriacetic acid nanofibers for tracking and enriching His-tagged proteins in living cells.
J Mater Chem B
; 9(1): 80-84, 2021 01 07.
Article
em En
| MEDLINE
| ID: mdl-33313613
ABSTRACT
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.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Oligopeptídeos
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Quelantes
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Citoplasma
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Nanofibras
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Histidina
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Ácido Nitrilotriacético
Limite:
Humans
Idioma:
En
Revista:
J Mater Chem B
Ano de publicação:
2021
Tipo de documento:
Article