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Encapsulins: Structure, Properties, and Biotechnological Applications

In 1994 a new class of prokaryotic compartments was discovered, collectively called “encapsulins” or “nanocompartments”. Encapsulin shell protomer proteins self-assemble to form icosahedral structures of various diameters (24-42 nm). Inside of nanocompartments shells, one or several cargo proteins,...

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Autores principales: Chmelyuk, Nelly S., Oda, Vera V., Gabashvili, Anna N., Abakumov, Maxim A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Pleiades Publishing 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9937530/
https://www.ncbi.nlm.nih.gov/pubmed/37068871
http://dx.doi.org/10.1134/S0006297923010042
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author Chmelyuk, Nelly S.
Oda, Vera V.
Gabashvili, Anna N.
Abakumov, Maxim A.
author_facet Chmelyuk, Nelly S.
Oda, Vera V.
Gabashvili, Anna N.
Abakumov, Maxim A.
author_sort Chmelyuk, Nelly S.
collection PubMed
description In 1994 a new class of prokaryotic compartments was discovered, collectively called “encapsulins” or “nanocompartments”. Encapsulin shell protomer proteins self-assemble to form icosahedral structures of various diameters (24-42 nm). Inside of nanocompartments shells, one or several cargo proteins, diverse in their functions, can be encapsulated. In addition, non-native cargo proteins can be loaded into nanocompartments, and shell surfaces can be modified via various compounds, which makes it possible to create targeted drug delivery systems, labels for optical and MRI imaging, and to use encapsulins as bioreactors. This review describes a number of strategies of encapsulins application in various fields of science, including biomedicine and nanobiotechnologies.
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spelling pubmed-99375302023-02-21 Encapsulins: Structure, Properties, and Biotechnological Applications Chmelyuk, Nelly S. Oda, Vera V. Gabashvili, Anna N. Abakumov, Maxim A. Biochemistry (Mosc) Review In 1994 a new class of prokaryotic compartments was discovered, collectively called “encapsulins” or “nanocompartments”. Encapsulin shell protomer proteins self-assemble to form icosahedral structures of various diameters (24-42 nm). Inside of nanocompartments shells, one or several cargo proteins, diverse in their functions, can be encapsulated. In addition, non-native cargo proteins can be loaded into nanocompartments, and shell surfaces can be modified via various compounds, which makes it possible to create targeted drug delivery systems, labels for optical and MRI imaging, and to use encapsulins as bioreactors. This review describes a number of strategies of encapsulins application in various fields of science, including biomedicine and nanobiotechnologies. Pleiades Publishing 2023-02-17 2023 /pmc/articles/PMC9937530/ /pubmed/37068871 http://dx.doi.org/10.1134/S0006297923010042 Text en © Pleiades Publishing, Ltd. 2023 This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.
spellingShingle Review
Chmelyuk, Nelly S.
Oda, Vera V.
Gabashvili, Anna N.
Abakumov, Maxim A.
Encapsulins: Structure, Properties, and Biotechnological Applications
title Encapsulins: Structure, Properties, and Biotechnological Applications
title_full Encapsulins: Structure, Properties, and Biotechnological Applications
title_fullStr Encapsulins: Structure, Properties, and Biotechnological Applications
title_full_unstemmed Encapsulins: Structure, Properties, and Biotechnological Applications
title_short Encapsulins: Structure, Properties, and Biotechnological Applications
title_sort encapsulins: structure, properties, and biotechnological applications
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9937530/
https://www.ncbi.nlm.nih.gov/pubmed/37068871
http://dx.doi.org/10.1134/S0006297923010042
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