ArticleChembiochem : a European journal of chemical biology2020
Efficient Generation of Hydrazides in Proteins by RadA Split Intein.
Article in Chembiochem : a European journal of chemical biology, 2020. 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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Who cites it
6 citing papers in PubMed, 8 citations in OpenAlex.
- Synthetic Strategies for Activity-Based Probes to Decode Ubiquitin-Like Modifiers.Chemistry (Weinheim an der Bergstrasse, Germany) · 2026Review
- Azole reagents enabled ligation of peptide acyl pyrazoles for chemical protein synthesis.Chemical science · 2024Article
- Semisynthesis of A6-A11 lactam insulin.Journal of peptide science : an official publication of the European Peptide Society · 2024Article
- A Shelf Stable Fmoc Hydrazine Resin for the Synthesis of Peptide Hydrazides.Peptide science (Hoboken, N.J.) · 2022Article
- Expressed Protein Selenoester Ligation.Angewandte Chemie (International ed. in English) · 2022Article
- Expressed Protein Selenoester Ligation.Angewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Protein C-terminal hydrazides are useful for bioconjugation and construction of proteins from multiple fragments through native chemical ligation. To generate C-terminal hydrazides in proteins, an efficient intein-based preparation method has been developed by using thiols and hydrazine to accelerate the formation of the transient thioester intermediate and subsequent hydrazinolysis. This approach not only increases the yield, but also improves biocompatibility. The scope of the method has been expanded by employing Pyrococcus horikoshii RadA split intein, which can accommodate a broad range of extein residues before the site of cleavage. The use of split RadA minimizes premature intein N cleavage in vivo and offers control over the initiation of the intein N cleavage reaction. It is expected that this versatile preparation method will expand the utilization of protein C-terminal hydrazides in protein preparation and modification.
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