ArticleFrontiers in chemistry2021
Chemical Synthesis of the Sec-To-Cys Homologue of Human Selenoprotein F and Elucidation of Its Disulfide-pairing Mode.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 12 citations in OpenAlex.
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Insights into the interaction between UGGT, the gatekeeper of folding in the ER, and its partner, the selenoprotein SEP15.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis.Chemical science · 2024Article
- A Shelf Stable Fmoc Hydrazine Resin for the Synthesis of Peptide Hydrazides.Peptide science (Hoboken, N.J.) · 2022Article
- Chemical synthesis of human selenoprotein F and elucidation of its thiol-disulfide oxidoreductase activity.Chemical science · 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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2 authors at 1 institution in 1 country.
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Abstract
Herein, we document a highly optimized synthesis of the Sec-to-Cys homologue of the human selenoprotein F (SelF) through a three-segment two-ligation semisynthesis strategy. Highlighted in this synthetic route are two one-pot manipulations, i.e. the first ligation followed by a desulfurization and the second ligation followed by the protein refolding. This way multi-milligrams of the folded synthetic protein was obtained, which set the stage for the synthesis of the natural selenoprotein. Moreover, the disulfide pairing mode of the SelF was elucidated through a combination of site-directed mutagenesis and LC-MS study. It provides not only a criterion to judge the viability of the synthetic protein, and more importantly, useful structural insights into the previously unresolved UGGT-binding domain of SelF.
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