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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,...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Pleiades Publishing
2023
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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. |
format | Online Article Text |
id | pubmed-9937530 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Pleiades Publishing |
record_format | MEDLINE/PubMed |
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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