ArticleACS nano2017
Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers: Nanopore Engineering and Characterization.
Article in ACS nano, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- Addressing the Challenges of Solid-State Nanopores: Strategies for Performance Enhancement.International journal of molecular sciences · 2026Review
- Computational methods and theory for ion channel research.Advances in physics: X · 2022Article
- The remarkable viral portal vertex: structure and a plausible model for mechanism.Current opinion in virology · 2021Review
- Rational ion transport management mediated through membrane structures.Exploration (Beijing, China) · 2021Review
- Biological Nanopores: Engineering on Demand.Life (Basel, Switzerland) · 2021Review
- Rapid and Accurate Determination of Nanopore Ionic Current Using a Steric Exclusion Model.ACS sensors · 2019Article
- Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors.Nature communications · 2018Article
- Nano-channel of viral DNA packaging motor as single pore to differentiate peptides with single amino acid difference.Biomaterials · 2018Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 3 countries.
Funding
Abstract
Nanopore-based sensors for nucleic acid sequencing and single-molecule detection typically employ pore-forming membrane proteins with hydrophobic external surfaces, suitable for insertion into a lipid bilayer. In contrast, hydrophilic pore-containing molecules, such as DNA origami, have been shown to require chemical modification to favor insertion into a lipid environment. In this work, we describe a strategy for inserting polar proteins with an inner pore into lipid membranes, focusing here on a circular 12-subunit assembly of the thermophage G20c portal protein. X-ray crystallography, electron microscopy, molecular dynamics, and thermal/chaotrope denaturation experiments all find the G20c portal protein to have a highly stable structure, favorable for nanopore sensing applications. Porphyrin conjugation to a cysteine mutant in the protein facilitates the protein's insertion into lipid bilayers, allowing us to probe ion transport through the pore. Finally, we probed the portal interior size and shape using a series of cyclodextrins of varying sizes, revealing asymmetric transport that possibly originates from the portal's DNA-ratchet function.
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Registered trials
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