Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions

Abstract 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)] prep...

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Main Authors: Mengmeng Zhou, Yutong Bi, Prof. Haijun Zhou, Xiaoqi Chen, Prof. Fen Zhang, Prof. Yantao Li, Prof. Xiongwei Qu
Format: Article
Language:English
Published: Wiley-VCH 2021-03-01
Series:ChemistryOpen
Subjects:
Online Access:https://doi.org/10.1002/open.202000336
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spelling doaj-38ee37e1b15d4c789979331bf74873f62021-08-26T16:40:26ZengWiley-VCHChemistryOpen2191-13632021-03-0110337337910.1002/open.202000336Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous SolutionsMengmeng Zhou0Yutong Bi1Prof. Haijun Zhou2Xiaoqi Chen3Prof. Fen Zhang4Prof. Yantao Li5Prof. Xiongwei Qu6School of Materials Science and Engineering Hebei University of Technology 300130 Tianjin ChinaSchool of Materials Science and Engineering Hebei University of Science and Technology 050000 Shijiazhuang Hebei Province ChinaInstitute of Energy Resources Hebei Academy of Sciences 050081 Shijiazhuang Hebei Province ChinaInstitute of Energy Resources Hebei Academy of Sciences 050081 Shijiazhuang Hebei Province ChinaInstitute of Energy Resources Hebei Academy of Sciences 050081 Shijiazhuang Hebei Province ChinaInstitute of Energy Resources Hebei Academy of Sciences 050081 Shijiazhuang Hebei Province ChinaSchool of Materials Science and Engineering Hebei University of Technology 300130 Tianjin ChinaAbstract 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.https://doi.org/10.1002/open.202000336aggregation behaviorbovine serum albuminhydrophobic interactionsmethacrylate derivativespolymers
collection DOAJ
language English
format Article
sources DOAJ
author Mengmeng Zhou
Yutong Bi
Prof. Haijun Zhou
Xiaoqi Chen
Prof. Fen Zhang
Prof. Yantao Li
Prof. Xiongwei Qu
spellingShingle Mengmeng Zhou
Yutong Bi
Prof. Haijun Zhou
Xiaoqi Chen
Prof. Fen Zhang
Prof. Yantao Li
Prof. Xiongwei Qu
Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions
ChemistryOpen
aggregation behavior
bovine serum albumin
hydrophobic interactions
methacrylate derivatives
polymers
author_facet Mengmeng Zhou
Yutong Bi
Prof. Haijun Zhou
Xiaoqi Chen
Prof. Fen Zhang
Prof. Yantao Li
Prof. Xiongwei Qu
author_sort Mengmeng Zhou
title 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_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_sort aggregation behavior of poly(acrylic acid‐co‐octadecyl methacrylate) and bovine serum albumin in aqueous solutions
publisher Wiley-VCH
series ChemistryOpen
issn 2191-1363
publishDate 2021-03-01
description Abstract 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.
topic aggregation behavior
bovine serum albumin
hydrophobic interactions
methacrylate derivatives
polymers
url https://doi.org/10.1002/open.202000336
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