The semisynthesis of nucleolar human selenoprotein H

Dardashti, Rebecca Notis; Laps, Shay; Gichtin, Jacob S.; Metanis, Norman

doi:10.1039/d3sc03059h

Chem. Sci.

2023

DOI: 10.1039/d3sc03059h

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The semisynthesis of nucleolar human selenoprotein H

Rebecca Notis Dardashti,

Shay Laps,

Jacob S. Gichtin

et al.

Abstract: The human selenoprotein H is the only selenocysteine-containing protein that is located in the cell’s nucleolus. In vivo studies have suggested that it plays some role in DNA binding, consumption...

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2024

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Cited by 2 publications

References 39 publications

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Biomimetic Folding Strategies for Chemical Synthesis of Disulfide‐Bonded Peptides and Proteins

Yu,

Zou,

Zheng

2024

ChemBioChem

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Disulfide‐bonded peptides and proteins, including hormones, toxins, growth factors, and others, are abundant in living organisms. These molecules play crucial physiological roles such as regulating cell and organism growth, development, and metabolism. They have also found widespread applications as drugs or tool molecules in biomedical and pharmaceutical research. However, the chemical synthesis of disulfide‐bonded proteins is complicated by the challenges associated with their folding. This review focuses on the latest advancements in disulfide‐bonded peptide and protein folding technologies. Particularly, it highlights biomimetic folding strategies that emulate the naturally occurring oxidative folding processes in nature. These strategies include chaperone‐assisted folding, glycosylation‐assisted folding, and organic‐based oxidative folding methods. The review also anticipates future directions in folding technology. Such research offers innovative approaches for the chemical synthesis of complex proteins that are otherwise difficult‐to‐fold.

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Biomimetic Folding Strategies for Chemical Synthesis of Disulfide‐Bonded Peptides and Proteins

Yu,

Zou,

Zheng

2024

ChemBioChem

View full text Add to dashboard Cite

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Encouraging Solution to the Problem of Synthesizing Protein α‐Thioester

Liu,

Gao,

Zhao

et al. 2024

Chin. J. Chem.

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Comprehensive SummaryExpressed protein ligation (EPL) provides a powerful tool to access large‐size proteins with precise structures. Existing methods for constructing the critical protein thioester for EPL have predominantly relied on the recombinant intein fusion expressed in Escherichia coli (E. coli). Despite its powerful applications, the expression of thioester derived from eukaryotic protein in E. coli inherently suffers from its limited solubility, the inactivity of intein, premature hydrolysis and low yields. To overcome these obstacles, we present herein the facile one‐flask synthesis of inaccessible protein α‐thioester via a SUMO‐protein‐intein (SPI) sandwich model. The utility of SUMO enhances the protein fusion yield and solubility, prevents premature hydrolysis and simplifies the purification process. The inaccessible protein thioester with internal Cys residues can be readily produced and is compatible with the EPL‐desulfurization protocol used to prepare complex proteins, which is otherwise difficult to obtain using traditional methods. Its utility has been highlighted through the synthesis of human granulocyte colony‐stimulating factor (G‐CSF).

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The semisynthesis of nucleolar human selenoprotein H

Abstract: The human selenoprotein H is the only selenocysteine-containing protein that is located in the cell’s nucleolus. In vivo studies have suggested that it plays some role in DNA binding, consumption...

Cited by 2 publications

References 39 publications

Biomimetic Folding Strategies for Chemical Synthesis of Disulfide‐Bonded Peptides and Proteins

Biomimetic Folding Strategies for Chemical Synthesis of Disulfide‐Bonded Peptides and Proteins

Encouraging Solution to the Problem of Synthesizing Protein α‐Thioester

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