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• W2899489314 abstract "Encapsulins are robust and engineerable proteins that form hollow, nanosized, icosahedral capsids, making them attractive vehicles for drug delivery, scaffolds for synthetic bionanoreactors, and artificial organelles. A major limitation of native encapsulins is the small size of pores in the protein shell. At 3 Å diameter, these pores impose significant restrictions on the molecular weight and diffusion rate of potential substrates. By redesigning the pore-forming loop region in encapsulin from Thermotoga maritima, we successfully enlarged pore diameter up to an estimated 11 Å and increased mass transport rates by 7-fold as measured by lanthanide ion diffusion assay. Our study demonstrates the high tolerance of encapsulin for protein engineering and has created a set of novel, functionally improved scaffolds for applications as bionanoreactors." @default.
• W2899489314 created "2018-11-09" @default.
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• W2899489314 date "2018-10-30" @default.
• W2899489314 modified "2023-10-01" @default.
• W2899489314 title "Pore Engineering for Enhanced Mass Transport in Encapsulin Nanocompartments" @default.
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• W2899489314 doi "https://doi.org/10.1021/acssynbio.8b00295" @default.
• W2899489314 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/30376298" @default.
• W2899489314 hasPublicationYear "2018" @default.
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