ArticleBioorganic & medicinal chemistry2018
In-cell production of a genetically-encoded library based on the θ-defensin RTD-1 using a bacterial expression system.
Article in Bioorganic & medicinal chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Resistance is futile: targeting multidrug-resistant bacteria withRSC chemical biology · 2023Review
- Efficient splicing of the CPE intein derived from directed evolution of theActa biochimica et biophysica Sinica · 2023Article
- Using the Cyclotide Scaffold for Targeting Biomolecular Interactions in Drug Development.Molecules (Basel, Switzerland) · 2022Review
- Scalable Biosynthetic Production of Knotted Peptides Enables ADME and Thermodynamic Folding Studies.ACS omega · 2021Article
- Engineered Cyclotides with Potent Broad in Vitro and in Vivo Antimicrobial Activity.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Using affinity propagation clustering for identifying bacterial clades and subclades with whole-genome sequences of Francisella tularensis.PLoS neglected tropical diseases · 2020Article
- The crystal structure of the naturally split gp41-1 intein guides the engineering of orthogonal split inteins from cis-splicing inteins.The FEBS journal · 2020Article
- Bacterial production and direct functional screening of expanded molecular libraries for discovering inhibitors of protein aggregation.Science advances · 2019Article
- Using backbone-cyclized Cys-rich polypeptides as molecular scaffolds to target protein-protein interactions.The Biochemical journal · 2019Review
- Biotechnological Applications of Protein Splicing.Current protein & peptide science · 2019Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
We report the high-yield heterologous expression of bioactive θ-defensin RTD-1 inside Escherichia coli cells by making use of intracellular protein trans-splicing in combination with a high efficient split-intein. RTD-1 is a small backbone-cyclized polypeptide with three disulfide bridges and a natural inhibitor of anthrax lethal factor protease. Recombinant RTD-1 was natively folded and able to inhibit anthrax lethal factor protease. In-cell expression of RTD-1 was very efficient and yielded ≈0.7mg of folded RTD-1 per gram of wet E. coli cells. This approach was used to generate of a genetically-encoded RTD-1-based peptide library in live E. coli cells. These results clearly demonstrate the possibility of using genetically-encoded RTD-1-based peptide libraries in live E. coli cells, which is a critical first step for developing in-cell screening and directed evolution technologies using the cyclic peptide RTD-1asa molecular scaffold.
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Registered trials
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.