ArticleNature communications2019
Enzymatic biosynthesis and immobilization of polyprotein verified at the single-molecule level.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
What it found
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Who cites it
40 citing papers in PubMed, 111 citations in OpenAlex.
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- Bridging Nature and Engineering: Protein-Derived Materials for Bio-Inspired Applications.Biomimetics (Basel, Switzerland) · 2024Review
- Tertiary amide bond formation by an engineered asparaginyl ligase.Chemical science · 2024Article
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- Red blood cell-derived materials for cancer therapy: Construction, distribution, and applications.Materials today. Bio · 2024Review
- Enzymatic Protein Immobilization for Nanobody Array.Molecules (Basel, Switzerland) · 2024Article
- S373P Mutation Stabilizes the Receptor-Binding Domain of the Spike Protein in Omicron and Promotes Binding.JACS Au · 2023Article
- OaAEP1 Ligase-Assisted Chemoenzymatic Synthesis of Full Cysteine-Rich Metal-Binding Cyanobacterial Metallothionein SmtA.Bioconjugate chemistry · 2023Article
- Carbon-Based Fluorescent Nano-Biosensors for the Detection of Cell-Free Circulating MicroRNAs.Biosensors · 2023Review
- Enzymatic Protein Immobilization on Amino-Functionalized Nanoparticles.Molecules (Basel, Switzerland) · 2023Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
Abstract
The recent development of chemical and bio-conjugation techniques allows for the engineering of various protein polymers. However, most of the polymerization process is difficult to control. To meet this challenge, we develop an enzymatic procedure to build polyprotein using the combination of a strict protein ligase OaAEP1 (Oldenlandia affinis asparaginyl endopeptidases 1) and a protease TEV (tobacco etch virus). We firstly demonstrate the use of OaAEP1-alone to build a sequence-uncontrolled ubiquitin polyprotein and covalently immobilize the coupled protein on the surface. Then, we construct a poly-metalloprotein, rubredoxin, from the purified monomer. Lastly, we show the feasibility of synthesizing protein polymers with rationally-controlled sequences by the synergy of the ligase and protease, which are verified by protein unfolding using atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS). Thus, this study provides a strategy for polyprotein engineering and immobilization.
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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.