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Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions
Polymer‐protein complexing systems have been extensively studied because of their wide application in biomedicine and industry. Here, we studied the aggregation behavior of the hydrophobically associating water‐soluble polymer poly(acrylic acid‐co‐octadecyl methacrylate) [P(AA‐co‐OMA)] prepared with...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7953483/ https://www.ncbi.nlm.nih.gov/pubmed/33629495 http://dx.doi.org/10.1002/open.202000336 |
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author | Zhou, Mengmeng Bi, Yutong Zhou, Haijun Chen, Xiaoqi Zhang, Fen Li, Yantao Qu, Xiongwei |
author_facet | Zhou, Mengmeng Bi, Yutong Zhou, Haijun Chen, Xiaoqi Zhang, Fen Li, Yantao Qu, Xiongwei |
author_sort | Zhou, Mengmeng |
collection | PubMed |
description | Polymer‐protein complexing systems have been extensively studied because of their wide application in biomedicine and industry. Here, we studied the aggregation behavior of the hydrophobically associating water‐soluble polymer poly(acrylic acid‐co‐octadecyl methacrylate) [P(AA‐co‐OMA)] prepared with nonionic surfactant as an emulsifier and bovine serum albumin (BSA) in aqueous solution. We identified the optimal composite conditions of P(AA‐co‐OMA) and BSA aqueous solution. We measured the zeta potential, dynamic light‐scattering particle size, and surface tension of P(AA‐co‐OMA) and BSA mixed aqueous solution. The results showed that the aggregation behavior between the polymer and BSA relied mainly on the hydrophobic interactions between the molecules. In addition, the best compounding condition was 8 wt.% of P(AA‐co‐OMA) content. The structure of hydrophobically associating polymer P(AA‐co‐OMA) and its aggregation with BSA were characterized by Fourier‐transform infrared spectroscopy. The infrared spectroscopy results identified the hydrogen bonding behavior of the amino and carboxyl groups between the polymer and BSA. This behavior was also confirmed using thermogravimetric analysis and differential scanning calorimetry. The thermal decomposition temperature and melting temperature of BSA changed before and after it was combined with the polymer. We measured the morphology of the polymer BSA aggregate with 8 % polymer content by transmission electron microscopy. The binding mechanism was investigated, as well. |
format | Online Article Text |
id | pubmed-7953483 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-79534832021-03-17 Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions Zhou, Mengmeng Bi, Yutong Zhou, Haijun Chen, Xiaoqi Zhang, Fen Li, Yantao Qu, Xiongwei ChemistryOpen Full Papers Polymer‐protein complexing systems have been extensively studied because of their wide application in biomedicine and industry. Here, we studied the aggregation behavior of the hydrophobically associating water‐soluble polymer poly(acrylic acid‐co‐octadecyl methacrylate) [P(AA‐co‐OMA)] prepared with nonionic surfactant as an emulsifier and bovine serum albumin (BSA) in aqueous solution. We identified the optimal composite conditions of P(AA‐co‐OMA) and BSA aqueous solution. We measured the zeta potential, dynamic light‐scattering particle size, and surface tension of P(AA‐co‐OMA) and BSA mixed aqueous solution. The results showed that the aggregation behavior between the polymer and BSA relied mainly on the hydrophobic interactions between the molecules. In addition, the best compounding condition was 8 wt.% of P(AA‐co‐OMA) content. The structure of hydrophobically associating polymer P(AA‐co‐OMA) and its aggregation with BSA were characterized by Fourier‐transform infrared spectroscopy. The infrared spectroscopy results identified the hydrogen bonding behavior of the amino and carboxyl groups between the polymer and BSA. This behavior was also confirmed using thermogravimetric analysis and differential scanning calorimetry. The thermal decomposition temperature and melting temperature of BSA changed before and after it was combined with the polymer. We measured the morphology of the polymer BSA aggregate with 8 % polymer content by transmission electron microscopy. The binding mechanism was investigated, as well. John Wiley and Sons Inc. 2021-02-25 /pmc/articles/PMC7953483/ /pubmed/33629495 http://dx.doi.org/10.1002/open.202000336 Text en © 2021 The Authors. Published by Wiley-VCH GmbH This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Full Papers Zhou, Mengmeng Bi, Yutong Zhou, Haijun Chen, Xiaoqi Zhang, Fen Li, Yantao Qu, Xiongwei Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title | Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title_full | Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title_fullStr | Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title_full_unstemmed | Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title_short | Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions |
title_sort | aggregation behavior of poly(acrylic acid‐co‐octadecyl methacrylate) and bovine serum albumin in aqueous solutions |
topic | Full Papers |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7953483/ https://www.ncbi.nlm.nih.gov/pubmed/33629495 http://dx.doi.org/10.1002/open.202000336 |
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