Site-specific covalent labeling of His-tag fused proteins with N-acyl-N-alkyl sulfonamide reagent

[Display omitted] The ability to incorporate a desired functionality into proteins of interest in a site-specific manner can provide powerful tools for investigating biological systems and creating therapeutic conjugates. However, there are not any universal methods that can be applied to all protei...

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Veröffentlicht in:Bioorganic & medicinal chemistry 2021-01, Vol.30, p.115947-115947, Article 115947
Hauptverfasser: Thimaradka, Vikram, Hoon Oh, Jae, Heroven, Christina, Radu Aricescu, A., Yuzaki, Michisuke, Tamura, Tomonori, Hamachi, Itaru
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container_end_page 115947
container_issue
container_start_page 115947
container_title Bioorganic & medicinal chemistry
container_volume 30
creator Thimaradka, Vikram
Hoon Oh, Jae
Heroven, Christina
Radu Aricescu, A.
Yuzaki, Michisuke
Tamura, Tomonori
Hamachi, Itaru
description [Display omitted] The ability to incorporate a desired functionality into proteins of interest in a site-specific manner can provide powerful tools for investigating biological systems and creating therapeutic conjugates. However, there are not any universal methods that can be applied to all proteins, and it is thus important to explore the chemical strategy for protein modification. In this paper, we developed a new reactive peptide tag/probe pair system for site-specific covalent protein labeling. This method relies on the recognition-driven reaction of a peptide tag and a molecular probe, which comprises the lysine-containing short histidine tag (KH6 or H6K) and a binuclear nickel (II)- nitrilotriacetic acid (Ni2+-NTA) complex probe containing a lysine-reactive N-acyl-N-alkyl sulfonamide (NASA) group. The selective interaction of the His-tag and Ni2+–NTA propeles a rapid nucleophilic reaction between a lysine residue of the tag and the electrophilic NASA group of the probe by the proximity effect, resulting in the tag-site-specific functionalization of proteins. We characterized the reactive profile and site-specificity of this method using model peptides and proteins in vitro, and demonstrated the general utility for production of a nanobody-chemical probe conjugate without compromising its binding ability.
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However, there are not any universal methods that can be applied to all proteins, and it is thus important to explore the chemical strategy for protein modification. In this paper, we developed a new reactive peptide tag/probe pair system for site-specific covalent protein labeling. This method relies on the recognition-driven reaction of a peptide tag and a molecular probe, which comprises the lysine-containing short histidine tag (KH6 or H6K) and a binuclear nickel (II)- nitrilotriacetic acid (Ni2+-NTA) complex probe containing a lysine-reactive N-acyl-N-alkyl sulfonamide (NASA) group. The selective interaction of the His-tag and Ni2+–NTA propeles a rapid nucleophilic reaction between a lysine residue of the tag and the electrophilic NASA group of the probe by the proximity effect, resulting in the tag-site-specific functionalization of proteins. 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ispartof Bioorganic & medicinal chemistry, 2021-01, Vol.30, p.115947-115947, Article 115947
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1464-3391
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source MEDLINE; Access via ScienceDirect (Elsevier)
subjects HEK293 Cells
Histidine - chemistry
Histidine - metabolism
Humans
Indicators and Reagents - chemistry
Indicators and Reagents - metabolism
Lysine - chemistry
Lysine - metabolism
Models, Molecular
Molecular Probes - chemistry
Molecular Probes - metabolism
Molecular Structure
Nickel - chemistry
Nickel - metabolism
Nitrilotriacetic Acid - chemistry
Nitrilotriacetic Acid - metabolism
Proteins - chemistry
Proteins - metabolism
Staining and Labeling
Sulfonamides - chemistry
Sulfonamides - metabolism
title Site-specific covalent labeling of His-tag fused proteins with N-acyl-N-alkyl sulfonamide reagent
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