ArticleNature protocols2017
Total chemical synthesis of histones and their analogs, assisted by native chemical ligation and palladium complexes.
Article in Nature protocols, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 46 citations in OpenAlex.
- Catalysis of Native Chemical Ligation and Expressed Protein Ligation by Alkylselenols.JACS Au · 2025Article
- Advances in the chemical synthesis of human proteoforms.Science China. Life sciences · 2025Review
- Interrogating epigenetic mechanisms with chemically customized chromatin.Nature reviews. Genetics · 2024Review
- OaAEP1 Ligase-Assisted Chemoenzymatic Synthesis of Full Cysteine-Rich Metal-Binding Cyanobacterial Metallothionein SmtA.Bioconjugate chemistry · 2023Article
- Histone H2B Deacylation Selectivity: Exploring Chromatin's Dark Matter with an Engineered Sortase.Journal of the American Chemical Society · 2022Article
- A glutamic acid-based traceless linker to address challenging chemical protein syntheses.Organic & biomolecular chemistry · 2021Article
- Diselenide-selenoester ligation for chemical protein synthesis.Nature protocols · 2019Article
- Cysteinylprolyl imide (CPI) peptide: a highly reactive and easily accessible crypto-thioester for chemical protein synthesis.Chemical science · 2019Article
- Diverse fate of ubiquitin chain moieties: The proximal is degraded with the target, and the distal protects the proximal from removal and recycles.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Palladium prompted on-demand cysteine chemistry for the synthesis of challenging and uniquely modified proteins.Nature communications · 2018Article
- Studies of biochemical crosstalk in chromatin with semisynthetic histones.Current opinion in chemical biology · 2018Review
- Total Chemical Synthesis of Modified Histones.Frontiers in chemistry · 2018Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Chemical synthesis of histones allows precise control of the installation of post-translational modifications via the coupling of derivatized amino acids. Shortcomings of other approaches for obtaining modified histones for epigenetic studies include heterogeneity of the obtained product and difficulties in incorporating multiple modifications on the same histone. In this protocol, unprotected peptide fragments are prepared by Fmoc solid-phase synthesis and coupled in aqueous buffers via native chemical ligation (NCL; in NCL, a peptide bond is formed between a peptide with an N-terminal Cys and another peptide having a C-terminal thioester). This task is challenging, with obstacles relating to the preparation and ligation of hydrophobic peptides, as well as the requirement for multiple purification steps due to protecting-group manipulations during the polypeptide assembly process. To address this, our approach uses an easily removable solubilizing tag for the synthesis and ligation of hydrophobic peptides, as well as a more efficient and better-yielding method to remove Cys-protecting groups that uses palladium chemistry (specifically [Pd(allyl)Cl]
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.