Cargando…

Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury

Spinal cord injury healing has been shown to be aided by chondroitinase ABC I (cABCI) treatment. The transport of cABCI to target tissues is complicated by the enzyme's thermal instability; however, cABCI may be immobilized on nanosheets to boost stability and improve delivery efficiency. This...

Descripción completa

Detalles Bibliográficos
Autores principales: Hassanli, Atefeh, Daneshjou, Sara, Dabirmanesh, Bahareh, Khajeh, Khosro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10600109/
https://www.ncbi.nlm.nih.gov/pubmed/37880390
http://dx.doi.org/10.1038/s41598-023-45555-9
_version_ 1785125916294250496
author Hassanli, Atefeh
Daneshjou, Sara
Dabirmanesh, Bahareh
Khajeh, Khosro
author_facet Hassanli, Atefeh
Daneshjou, Sara
Dabirmanesh, Bahareh
Khajeh, Khosro
author_sort Hassanli, Atefeh
collection PubMed
description Spinal cord injury healing has been shown to be aided by chondroitinase ABC I (cABCI) treatment. The transport of cABCI to target tissues is complicated by the enzyme's thermal instability; however, cABCI may be immobilized on nanosheets to boost stability and improve delivery efficiency. This investigation's goal was to assess the immobilization of cABC I on graphene oxide (GO). for this purpose, GO was produced from graphene using a modified version of Hummer’s process. the immobilization of cABC I on GO was examined using SEM, XRD, and FTIR. The enzymatic activity of cABC I was evaluated in relation to substrate concentration. The enzyme was then surface-adsorption immobilized on GO, and its thermal stability was examined. As compared to the free enzyme, the results showed that the immobilized enzyme had a greater Km and a lower Vmax value. The stability of the enzyme was greatly improved by immobilization at 20, 4, 25, and 37 °C. For example, at 37 °C, the free enzyme retained 5% of its activity after 100 min, while the immobilized one retained 30% of its initial activity. The results showed, As a suitable surface for immobilizing cABC I, GO nano sheets boost the enzyme's stability, improving its capability to support axonal regeneration after CNC damage and guard against fast degradation.
format Online
Article
Text
id pubmed-10600109
institution National Center for Biotechnology Information
language English
publishDate 2023
publisher Nature Publishing Group UK
record_format MEDLINE/PubMed
spelling pubmed-106001092023-10-27 Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury Hassanli, Atefeh Daneshjou, Sara Dabirmanesh, Bahareh Khajeh, Khosro Sci Rep Article Spinal cord injury healing has been shown to be aided by chondroitinase ABC I (cABCI) treatment. The transport of cABCI to target tissues is complicated by the enzyme's thermal instability; however, cABCI may be immobilized on nanosheets to boost stability and improve delivery efficiency. This investigation's goal was to assess the immobilization of cABC I on graphene oxide (GO). for this purpose, GO was produced from graphene using a modified version of Hummer’s process. the immobilization of cABC I on GO was examined using SEM, XRD, and FTIR. The enzymatic activity of cABC I was evaluated in relation to substrate concentration. The enzyme was then surface-adsorption immobilized on GO, and its thermal stability was examined. As compared to the free enzyme, the results showed that the immobilized enzyme had a greater Km and a lower Vmax value. The stability of the enzyme was greatly improved by immobilization at 20, 4, 25, and 37 °C. For example, at 37 °C, the free enzyme retained 5% of its activity after 100 min, while the immobilized one retained 30% of its initial activity. The results showed, As a suitable surface for immobilizing cABC I, GO nano sheets boost the enzyme's stability, improving its capability to support axonal regeneration after CNC damage and guard against fast degradation. Nature Publishing Group UK 2023-10-25 /pmc/articles/PMC10600109/ /pubmed/37880390 http://dx.doi.org/10.1038/s41598-023-45555-9 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Hassanli, Atefeh
Daneshjou, Sara
Dabirmanesh, Bahareh
Khajeh, Khosro
Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title_full Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title_fullStr Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title_full_unstemmed Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title_short Improvement of thermal-stability of chondroitinase ABCI immobilized on graphene oxide for the repair of spinal cord injury
title_sort improvement of thermal-stability of chondroitinase abci immobilized on graphene oxide for the repair of spinal cord injury
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10600109/
https://www.ncbi.nlm.nih.gov/pubmed/37880390
http://dx.doi.org/10.1038/s41598-023-45555-9
work_keys_str_mv AT hassanliatefeh improvementofthermalstabilityofchondroitinaseabciimmobilizedongrapheneoxidefortherepairofspinalcordinjury
AT daneshjousara improvementofthermalstabilityofchondroitinaseabciimmobilizedongrapheneoxidefortherepairofspinalcordinjury
AT dabirmaneshbahareh improvementofthermalstabilityofchondroitinaseabciimmobilizedongrapheneoxidefortherepairofspinalcordinjury
AT khajehkhosro improvementofthermalstabilityofchondroitinaseabciimmobilizedongrapheneoxidefortherepairofspinalcordinjury