Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities

Zhuofu Wu, 1, 2 Sitong Zhang, 1 Xiaojun Wang, 2 Can Cai, 2 Guang Chen, 1 Li Ma 2 1Key Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, People’s Republic of China; 2Department of Physics, Geor...

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Autores principales:	Wu Z, Zhang S, Wang X, Cai C, Chen G, Ma L
Formato:	article
Lenguaje:	EN
Publicado:	Dove Medical Press 2020
Materias:	catalase superoxide dismutase polynitroxylated human serum albumin reactive oxygen species Medicine (General) R5-920
Acceso en línea:	https://doaj.org/article/537f764a351445469cc5f5e02cebeb38
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spelling	oai:doaj.org-article:537f764a351445469cc5f5e02cebeb382021-12-02T04:41:45ZNitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities1178-2013https://doaj.org/article/537f764a351445469cc5f5e02cebeb382020-01-01T00:00:00Zhttps://www.dovepress.com/nitroxide-modified-protein-incorporated-nanoflowers-with-dual-enzyme-l-peer-reviewed-article-IJNhttps://doaj.org/toc/1178-2013Zhuofu Wu, 1, 2 Sitong Zhang, 1 Xiaojun Wang, 2 Can Cai, 2 Guang Chen, 1 Li Ma 2 1Key Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, People’s Republic of China; 2Department of Physics, Georgia Southern University, Statesboro, GA 30460, USACorrespondence: Guang ChenCollege of Life Science, Jilin Agricultural University, No. 2888 Xincheng Avenue, Changchun 130118, People’s Republic of ChinaTel/Fax +86 431 8453 2942Email guangc61@gmail.com Li MaDepartment of Physics, Georgia Southern University, 65 Georgia Avenue, Math/Physics Building Room 1003, Statesboro, GA 30460, USATel +1 912 478 5950Fax +1 912 478 0471Email lma@GeorgiaSouthern.eduPurpose: Combined superoxide dismutase (SOD)/catalase mimetics have attracted much attention because of their efficacy against reactive oxygen species-associated diseases; however, their application is often limited owing to their poor stability and the absence of favorable grafting sites. To address this, we developed a new class of SOD/catalase mimetics based on hybrid nanoflowers, which exhibit superior stability and possess the desired grafting sites for drugs and endogenous molecules.Methods: In this work, for the first time, we used polynitroxylated human serum albumin (PNA) to mediate the formation of hybrid copper-based nanoflowers. H 2O 2 depletion and O 2 evolution assays were first performed to determine the catalase-like activity of the hybrid nanoflowers. Next, the xanthine oxidase/cytochrome c method was used to assay the SOD-like activity of the nanoflowers. Further characteristics of the nanoflowers were evaluated using scanning electron microscopy (SEM), electron paramagnetic resonance (EPR), and Fourier-transform infrared spectroscopy (FTIR). Operational stability was assessed via the reusability assay.Results: The H 2O 2 depletion and O 2 evolution assays indicated that PNA-incorporated nanoflowers have genuine catalase-like activity. Kinetic analysis revealed that the reactions of the incorporated nanoflowers with H 2O 2 not only obey Michaelis–Menton kinetics, but that the nanoflowers also possess a higher affinity for H 2O 2 than that of native catalase. The FTIR spectra corroborated the presence of PNA in the hybrid nanoflowers, while the EPR spectra confirmed the intermolecular interaction of nitroxides bound to the human serum albumin incorporated into the nanoflowers. The remarkable operational reproducibility of the hybrid nanoflowers in catalase-like and SOD-like reactions was verified across successive batches.Conclusion: Herein, a comparison of Michaelis constants showed that the hybrid nanoflower, a catalase mimetics, outperforms the native catalase. Acting as a “better-than-nature” enzyme mimetics, the hybrid nanoflower with superior stability and desired ligand grafting sites will find widespread utilization in the medical sciences.Keywords: catalase, superoxide dismutase, polynitroxylated human serum albumin, reactive oxygen species, copper-based nanoflowersWu ZZhang SWang XCai CChen GMa LDove Medical Pressarticlecatalasesuperoxide dismutasepolynitroxylated human serum albuminreactive oxygen speciesMedicine (General)R5-920ENInternational Journal of Nanomedicine, Vol Volume 15, Pp 263-273 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	catalase superoxide dismutase polynitroxylated human serum albumin reactive oxygen species Medicine (General) R5-920
spellingShingle	catalase superoxide dismutase polynitroxylated human serum albumin reactive oxygen species Medicine (General) R5-920 Wu Z Zhang S Wang X Cai C Chen G Ma L Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
description	Zhuofu Wu, 1, 2 Sitong Zhang, 1 Xiaojun Wang, 2 Can Cai, 2 Guang Chen, 1 Li Ma 2 1Key Laboratory of Straw Biology and Utilization, The Ministry of Education, College of Life Science, Jilin Agricultural University, Changchun 130118, People’s Republic of China; 2Department of Physics, Georgia Southern University, Statesboro, GA 30460, USACorrespondence: Guang ChenCollege of Life Science, Jilin Agricultural University, No. 2888 Xincheng Avenue, Changchun 130118, People’s Republic of ChinaTel/Fax +86 431 8453 2942Email guangc61@gmail.com Li MaDepartment of Physics, Georgia Southern University, 65 Georgia Avenue, Math/Physics Building Room 1003, Statesboro, GA 30460, USATel +1 912 478 5950Fax +1 912 478 0471Email lma@GeorgiaSouthern.eduPurpose: Combined superoxide dismutase (SOD)/catalase mimetics have attracted much attention because of their efficacy against reactive oxygen species-associated diseases; however, their application is often limited owing to their poor stability and the absence of favorable grafting sites. To address this, we developed a new class of SOD/catalase mimetics based on hybrid nanoflowers, which exhibit superior stability and possess the desired grafting sites for drugs and endogenous molecules.Methods: In this work, for the first time, we used polynitroxylated human serum albumin (PNA) to mediate the formation of hybrid copper-based nanoflowers. H 2O 2 depletion and O 2 evolution assays were first performed to determine the catalase-like activity of the hybrid nanoflowers. Next, the xanthine oxidase/cytochrome c method was used to assay the SOD-like activity of the nanoflowers. Further characteristics of the nanoflowers were evaluated using scanning electron microscopy (SEM), electron paramagnetic resonance (EPR), and Fourier-transform infrared spectroscopy (FTIR). Operational stability was assessed via the reusability assay.Results: The H 2O 2 depletion and O 2 evolution assays indicated that PNA-incorporated nanoflowers have genuine catalase-like activity. Kinetic analysis revealed that the reactions of the incorporated nanoflowers with H 2O 2 not only obey Michaelis–Menton kinetics, but that the nanoflowers also possess a higher affinity for H 2O 2 than that of native catalase. The FTIR spectra corroborated the presence of PNA in the hybrid nanoflowers, while the EPR spectra confirmed the intermolecular interaction of nitroxides bound to the human serum albumin incorporated into the nanoflowers. The remarkable operational reproducibility of the hybrid nanoflowers in catalase-like and SOD-like reactions was verified across successive batches.Conclusion: Herein, a comparison of Michaelis constants showed that the hybrid nanoflower, a catalase mimetics, outperforms the native catalase. Acting as a “better-than-nature” enzyme mimetics, the hybrid nanoflower with superior stability and desired ligand grafting sites will find widespread utilization in the medical sciences.Keywords: catalase, superoxide dismutase, polynitroxylated human serum albumin, reactive oxygen species, copper-based nanoflowers
format	article
author	Wu Z Zhang S Wang X Cai C Chen G Ma L
author_facet	Wu Z Zhang S Wang X Cai C Chen G Ma L
author_sort	Wu Z
title	Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
title_short	Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
title_full	Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
title_fullStr	Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
title_full_unstemmed	Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities
title_sort	nitroxide-modified protein-incorporated nanoflowers with dual enzyme-like activities
publisher	Dove Medical Press
publishDate	2020
url	https://doaj.org/article/537f764a351445469cc5f5e02cebeb38
work_keys_str_mv	AT wuz nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities AT zhangs nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities AT wangx nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities AT caic nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities AT cheng nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities AT mal nitroxidemodifiedproteinincorporatednanoflowerswithdualenzymelikeactivities
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Nitroxide-Modified Protein-Incorporated Nanoflowers with Dual Enzyme-Like Activities

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