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Site-Specific and Trigger-Activated Modification of Proteins by Means of Catalytic Hemin/G-quadruplex DNAzyme Nanostructures.

ABSTRACT: Catalytic nanostructures have the potency to mimic enzymatic features. In this paper, we show that the complex between hemin and G-quadruplex DNA efficiently catalyzes the modification of proteins with N-methyl luminol derivatives. Final conversions are reached within 15-30 min, and LC-MS analysis of tryptic digests of the proteins shows that the reaction proceeds with chemoselectivity for electron-rich aromatic residues (Tyr ? Trp), and the site-specificity of the modification depends on the sequence and secondary structure folding of the G-quadruplex nanostructure. Furthermore, the modification can be applied on proteins with different biomedical functions, and the nanostructure can be designed to contain a regulatory element in order to regulate protein modification by an external stimulus.

SUBMITTER: Keijzer JF

PROVIDER: S-EPMC7581286 | biostudies-literature | 2020 Oct

REPOSITORIES: biostudies-literature

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Site-Specific and Trigger-Activated Modification of Proteins by Means of Catalytic Hemin/G-quadruplex DNAzyme Nanostructures.

Keijzer Jordi F JF Albada Bauke B

Bioconjugate chemistry 20200918 10

Catalytic nanostructures have the potency to mimic enzymatic features. In this paper, we show that the complex between hemin and G-quadruplex DNA efficiently catalyzes the modification of proteins with <i>N</i>-methyl luminol derivatives. Final conversions are reached within 15-30 min, and LC-MS analysis of tryptic digests of the proteins shows that the reaction proceeds with chemoselectivity for electron-rich aromatic residues (Tyr ≫ Trp), and the site-specificity of the modification depends on ...[more]

PMID: 32909740

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