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Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity

Accurately detecting dynamic changes in bioactive small molecules in real-time is very challenging. In this study, a hemin-based peptide assembly was rationally designed for the colorimetric detection of active small molecules. Hemin-functionalized peptide nanotubes were obtained through the direct...

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Autores principales: Xiang, Song, Long, Xincheng, Tu, Qiuxia, Feng, Jian, Zhang, Xiaohe, Feng, Guangwei, Lei, Li
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Nature Singapore 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9899300/
https://www.ncbi.nlm.nih.gov/pubmed/36738341
http://dx.doi.org/10.1186/s40580-023-00356-8
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author Xiang, Song
Long, Xincheng
Tu, Qiuxia
Feng, Jian
Zhang, Xiaohe
Feng, Guangwei
Lei, Li
author_facet Xiang, Song
Long, Xincheng
Tu, Qiuxia
Feng, Jian
Zhang, Xiaohe
Feng, Guangwei
Lei, Li
author_sort Xiang, Song
collection PubMed
description Accurately detecting dynamic changes in bioactive small molecules in real-time is very challenging. In this study, a hemin-based peptide assembly was rationally designed for the colorimetric detection of active small molecules. Hemin-functionalized peptide nanotubes were obtained through the direct incubation of hemin (hemin@PNTs) and peptide nanotubes (PNTs) or were coassembled with the heptapeptide Ac-KLVFFAL-NH(2) via electrostatic, π–π stacking, and hydrophobic interactions (hemin-PNTs). This new substance is significant because it exhibits the benefits of both hemin and PNTs as well as some special qualities. First, hemin-PNTs exhibited higher intrinsic peroxidase-like activity, which, in the presence of H(2)O(2), could catalyze the oxidation of the substrate 3,3',5,5'-tetramethylbenzidine (TMB) to yield a typical blue solution after 10 min at 25 ℃. Second, hemin-PNTs showed significantly higher activity than that of hemin, PNTs alone, or hemin@PNTs. Hemin-PNTs with a 20.0% hemin content may cooperate to improve catalytic activity. The catalytic activity was dependent on the reaction temperature, pH, reaction time, and H(2)O(2) concentration. The nature of the TMB-catalyzed reaction may arise from the production of hydroxyl radicals. Fluorescence analysis was used to demonstrate the catalytic mechanism. According to this investigation, a new highly selective and sensitive colorimetric technique for detecting glutathione (GSH), L-cysteine, and glucose was established. The strategy demonstrated excellent sensitivity for GSH in the range of 1 to 30 μM with a 0.51 μM detection limit. Importantly, this glucose detection technique, which employs glucose oxidase and hemin-PNTs, is simple and inexpensive, with a 0.1 μM to 1.0 mM linear range and a 15.2 μM detection limit. Because of their low cost and high catalytic activity, hemin-PNTs are an excellent choice for biocatalysts in a diverse range of potential applications, including applications in clinical diagnostics, environmental chemistry, and biotechnology. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s40580-023-00356-8.
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spelling pubmed-98993002023-02-06 Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity Xiang, Song Long, Xincheng Tu, Qiuxia Feng, Jian Zhang, Xiaohe Feng, Guangwei Lei, Li Nano Converg Full Paper Accurately detecting dynamic changes in bioactive small molecules in real-time is very challenging. In this study, a hemin-based peptide assembly was rationally designed for the colorimetric detection of active small molecules. Hemin-functionalized peptide nanotubes were obtained through the direct incubation of hemin (hemin@PNTs) and peptide nanotubes (PNTs) or were coassembled with the heptapeptide Ac-KLVFFAL-NH(2) via electrostatic, π–π stacking, and hydrophobic interactions (hemin-PNTs). This new substance is significant because it exhibits the benefits of both hemin and PNTs as well as some special qualities. First, hemin-PNTs exhibited higher intrinsic peroxidase-like activity, which, in the presence of H(2)O(2), could catalyze the oxidation of the substrate 3,3',5,5'-tetramethylbenzidine (TMB) to yield a typical blue solution after 10 min at 25 ℃. Second, hemin-PNTs showed significantly higher activity than that of hemin, PNTs alone, or hemin@PNTs. Hemin-PNTs with a 20.0% hemin content may cooperate to improve catalytic activity. The catalytic activity was dependent on the reaction temperature, pH, reaction time, and H(2)O(2) concentration. The nature of the TMB-catalyzed reaction may arise from the production of hydroxyl radicals. Fluorescence analysis was used to demonstrate the catalytic mechanism. According to this investigation, a new highly selective and sensitive colorimetric technique for detecting glutathione (GSH), L-cysteine, and glucose was established. The strategy demonstrated excellent sensitivity for GSH in the range of 1 to 30 μM with a 0.51 μM detection limit. Importantly, this glucose detection technique, which employs glucose oxidase and hemin-PNTs, is simple and inexpensive, with a 0.1 μM to 1.0 mM linear range and a 15.2 μM detection limit. Because of their low cost and high catalytic activity, hemin-PNTs are an excellent choice for biocatalysts in a diverse range of potential applications, including applications in clinical diagnostics, environmental chemistry, and biotechnology. SUPPLEMENTARY INFORMATION: The online version contains supplementary material available at 10.1186/s40580-023-00356-8. Springer Nature Singapore 2023-02-04 /pmc/articles/PMC9899300/ /pubmed/36738341 http://dx.doi.org/10.1186/s40580-023-00356-8 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open AccessThis 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 Full Paper
Xiang, Song
Long, Xincheng
Tu, Qiuxia
Feng, Jian
Zhang, Xiaohe
Feng, Guangwei
Lei, Li
Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title_full Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title_fullStr Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title_full_unstemmed Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title_short Self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
title_sort self-assembled, hemin-functionalized peptide nanotubes: an innovative strategy for detecting glutathione and glucose molecules with peroxidase-like activity
topic Full Paper
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9899300/
https://www.ncbi.nlm.nih.gov/pubmed/36738341
http://dx.doi.org/10.1186/s40580-023-00356-8
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