Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions. Issue 3 (25th February 2021)
- Record Type:
- Journal Article
- Title:
- Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions. Issue 3 (25th February 2021)
- Main Title:
- Aggregation Behavior of Poly(Acrylic acid‐co‐Octadecyl Methacrylate) and Bovine Serum Albumin in Aqueous Solutions
- Authors:
- Zhou, Mengmeng
Bi, Yutong
Zhou, Haijun
Chen, Xiaoqi
Zhang, Fen
Li, Yantao
Qu, Xiongwei - Abstract:
- 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 electronAbstract: 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. Abstract : The aggregation behavior between P(AA‐co‐OMA) and BSA, which primarily depends on hydrophobic aggregation and hydrogen‐bonding interaction, has been investigated. As shown in the figure, the gray area reveals that the hydrophobic regions of P(AA‐co‐OMA) and BSA gather together, and the hydrophilic areas are located next to each other as a result of the hydrogen‐bonding interaction. … (more)
- Is Part Of:
- ChemistryOpen. Volume 10:Issue 3(2021)
- Journal:
- ChemistryOpen
- Issue:
- Volume 10:Issue 3(2021)
- Issue Display:
- Volume 10, Issue 3 (2021)
- Year:
- 2021
- Volume:
- 10
- Issue:
- 3
- Issue Sort Value:
- 2021-0010-0003-0000
- Page Start:
- 373
- Page End:
- 379
- Publication Date:
- 2021-02-25
- Subjects:
- aggregation behavior -- bovine serum albumin -- hydrophobic interactions -- methacrylate derivatives -- polymers
Chemistry -- Periodicals
540
540.5 - Journal URLs:
- http://onlinelibrary.wiley.com/journal/10.1002/(ISSN)2191-1363 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/open.202000336 ↗
- Languages:
- English
- ISSNs:
- 2191-1363
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 26149.xml