Sub-micro- and nano-sized polyethylene terephthalate deconstruction with engineered protein nanopores
Creators
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Robles Martín, Ana
(Researcher)1
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Amigot Sánchez, Rafael
(Researcher)2
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Fernandez-Lopez, Laura
(Researcher)3
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González Alfonso, José Luis
(Researcher)3
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Roda, Sergi
(Researcher)1
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Alcolea-Rodriguez, Victor
(Researcher)3
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Heras Márquez, Diego
(Researcher)2
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Almendral Nieto, David
(Researcher)3
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Coscolín, Cristina
(Researcher)3
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Plou, Francisco J.
(Supervisor)3
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Portela, Raquel
(Supervisor)4
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Bañares, Miguel A.
(Supervisor)5, 6
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Martinez-del-Pozo, Alvaro
(Supervisor)2
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García Linares, Sara
(Supervisor)2
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Ferrer, Manuel
(Supervisor)7
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Guallar, Victor
(Supervisor)8, 1
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1.
Barcelona Supercomputing Center
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2.
Universidad Complutense de Madrid
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3.
Instituto de Catálisis y Petroleoquímica
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4.
Consejo Superior de Investigaciones Científicas
- 5. CSIC, Consejo Superior de Investigaciones Cientificas
- 6. CSIC
- 7. Institute of Catalysis - CSIC
- 8. ICREA -Institucio Catalana de Recerca i Estudis Avançats
Description
The identification or design of biocatalysts to mitigate the accumulation of plastics, including sub-micro- and nano-sized polyethylene terephthalate (nPET), is becoming a global challenge. Here we computationally incorporated two hydrolytic active sites with geometries similar to that of Idionella sakaiensis PET hydrolase, to fragaceatoxin C (FraC), a membrane pore-forming protein. FraCm1/m2 could be assembled into octameric nanopores (7.0 nm high × 1.6–6.0 nm entry), which deconstructed (40 °C, pH 7.0) nPET from GoodFellow, commodities and plastic bottles. FraCm1 and FraCm2 degrade nPET by endo- and exo-type chain scission. While FraCm1 produces bis(2-hydroxyethyl) terephthalate as the main product, FraCm2 yields a high diversity of oligomers and terephthalic acid. Mechanistic and biochemical differences with benchmark PET hydrolases, along with pore and nPET dynamics, suggest that these pore-forming protein catalytic nanoreactors do not deconstruct macro-PET but are promising in nanotechnology for filtering, capturing and breaking down nPET, for example, in wastewater treatment plants.
Files
Raw MS data Supp 14_NatCal2023.zip
Files
(216.3 MB)
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Additional details
Related works
- Is supplement to
- Journal article: 10.1038/s41929-023-01048-6 (DOI)
Funding
- European Commission
- FuturEnzyme - Technologies of the Future for Low-Cost Enzymes for Environment-Friendly Products 101000327
- European Commission
- NYMPHE - New system-driven bioremediation of polluted habitats and environment 101060625
- European Commission
- PlasticsFatE - Plastics fate and effects in the human body 965367