ArticleCommunications chemistry2021
Diselenide crosslinks for enhanced and simplified oxidative protein folding.
Article in Communications chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Effects of Selenocysteine Substitution on the Cyclotide Kalata B2.Chembiochem : a European journal of chemical biology · 2026Article
- Replacing of Cysteine with Selenocysteine: Biochemical Considerations, Computational Modeling, and Protein Engineering Applications.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Directing the oxidative folding of disulfide-rich peptides for enhanced engineering and applications.Chemical science · 2025Review
- Comparative Study of Hirudins and Encoding Genes inBiology · 2025Article
- Advances in Peptidomimetics for Next-Generation Therapeutics: Strategies, Modifications, and Applications.Chemical reviews · 2025Review
- Seleno-relaxin analogues: effect of internal and external diselenide bonds on the foldability and a fibrosis-related factor of endometriotic stromal cells.RSC chemical biology · 2024Article
- Organic solvent enhances oxidative folding of disulfide-rich proteins.Nature chemistry · 2024Article
- Photochemical Transformations of Peptides Containing theACS omega · 2024Article
- Selenium chemistry for spatio-selective peptide and protein functionalization.Nature reviews. Chemistry · 2024Review
- Diselenide-bond replacement of the external disulfide bond of insulin increases its oligomerization leading to sustained activity.Communications chemistry · 2023Article
- The semisynthesis of nucleolar human selenoprotein H.Chemical science · 2023Article
- Revisiting the Asian Buffalo Leech (Genes · 2023Article
- A Chemoenzymatic Approach To Produce a Cyclic Analogue of the Analgesic Drug MVIIA (Ziconotide).Angewandte Chemie (International ed. in English) · 2023Article
- Selenium in Peptide Chemistry.Molecules (Basel, Switzerland) · 2023Review
- A Shelf Stable Fmoc Hydrazine Resin for the Synthesis of Peptide Hydrazides.Peptide science (Hoboken, N.J.) · 2022Article
- One-Pot Chemical Protein Synthesis Utilizing Fmoc-Masked Selenazolidine to Address the Redox Functionality of Human Selenoprotein F.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
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Authors and funding
8 authors.
Funding
Abstract
The in vitro oxidative folding of proteins has been studied for over sixty years, providing critical insight into protein folding mechanisms. Hirudin, the most potent natural inhibitor of thrombin, is a 65-residue protein with three disulfide bonds, and is viewed as a folding model for a wide range of disulfide-rich proteins. Hirudin's folding pathway is notorious for its highly heterogeneous intermediates and scrambled isomers, limiting its folding rate and yield in vitro. Aiming to overcome these limitations, we undertake systematic investigation of diselenide bridges at native and non-native positions and investigate their effect on hirudin's folding, structure and activity. Our studies demonstrate that, regardless of the specific positions of these substitutions, the diselenide crosslinks enhanced the folding rate and yield of the corresponding hirudin analogues, while reducing the complexity and heterogeneity of the process. Moreover, crystal structure analysis confirms that the diselenide substitutions maintained the overall three-dimensional structure of the protein and left its function virtually unchanged. The choice of hirudin as a study model has implications beyond its specific folding mechanism, demonstrating the high potential of diselenide substitutions in the design, preparation and characterization of disulfide-rich proteins.
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Registered trials
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