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Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid

Ribonuclease S (RNase S) is an enzyme that exhibits anticancer activity by degrading RNAs within cancer cells; however, the cellular uptake efficiency is low due to its small molecular size. Here we generated RNase S‐decorated artificial viral capsids with a size of 70–170 nm by self‐assembly of the...

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Autores principales: Liang, Yingbing, Furukawa, Hiroto, Sakamoto, Kentarou, Inaba, Hiroshi, Matsuura, Kazunori
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9400862/
https://www.ncbi.nlm.nih.gov/pubmed/35676201
http://dx.doi.org/10.1002/cbic.202200220
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author Liang, Yingbing
Furukawa, Hiroto
Sakamoto, Kentarou
Inaba, Hiroshi
Matsuura, Kazunori
author_facet Liang, Yingbing
Furukawa, Hiroto
Sakamoto, Kentarou
Inaba, Hiroshi
Matsuura, Kazunori
author_sort Liang, Yingbing
collection PubMed
description Ribonuclease S (RNase S) is an enzyme that exhibits anticancer activity by degrading RNAs within cancer cells; however, the cellular uptake efficiency is low due to its small molecular size. Here we generated RNase S‐decorated artificial viral capsids with a size of 70–170 nm by self‐assembly of the β‐annulus‐S‐peptide followed by reconstitution with S‐protein at neutral pH. The RNase S‐decorated artificial viral capsids are efficiently taken up by HepG2 cells and exhibit higher RNA degradation activity in cells compared with RNase S alone. Cell viability assays revealed that RNase S‐decorated capsids have high anticancer activity comparable to that of standard anticancer drugs.
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spelling pubmed-94008622022-08-26 Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid Liang, Yingbing Furukawa, Hiroto Sakamoto, Kentarou Inaba, Hiroshi Matsuura, Kazunori Chembiochem Research Articles Ribonuclease S (RNase S) is an enzyme that exhibits anticancer activity by degrading RNAs within cancer cells; however, the cellular uptake efficiency is low due to its small molecular size. Here we generated RNase S‐decorated artificial viral capsids with a size of 70–170 nm by self‐assembly of the β‐annulus‐S‐peptide followed by reconstitution with S‐protein at neutral pH. The RNase S‐decorated artificial viral capsids are efficiently taken up by HepG2 cells and exhibit higher RNA degradation activity in cells compared with RNase S alone. Cell viability assays revealed that RNase S‐decorated capsids have high anticancer activity comparable to that of standard anticancer drugs. John Wiley and Sons Inc. 2022-06-21 2022-08-03 /pmc/articles/PMC9400862/ /pubmed/35676201 http://dx.doi.org/10.1002/cbic.202200220 Text en © 2022 The Authors. ChemBioChem published by Wiley-VCH GmbH https://creativecommons.org/licenses/by-nc/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ (https://creativecommons.org/licenses/by-nc/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.
spellingShingle Research Articles
Liang, Yingbing
Furukawa, Hiroto
Sakamoto, Kentarou
Inaba, Hiroshi
Matsuura, Kazunori
Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title_full Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title_fullStr Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title_full_unstemmed Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title_short Anticancer Activity of Reconstituted Ribonuclease S‐Decorated Artificial Viral Capsid
title_sort anticancer activity of reconstituted ribonuclease s‐decorated artificial viral capsid
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9400862/
https://www.ncbi.nlm.nih.gov/pubmed/35676201
http://dx.doi.org/10.1002/cbic.202200220
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