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Dual Thermo- and pH-Responsive Behavior of Double Zwitterionic Graft Copolymers for Suppression of Protein Aggregation and Protein Release
- Source :
- ACS Applied Materials & Interfaces. 11:39459-39469
- Publication Year :
- 2019
- Publisher :
- American Chemical Society (ACS), 2019.
-
Abstract
- Graft copolymers consisting of two different zwitterionic blocks were synthesized via reversible addition fragmentation chain transfer polymerization. These polymers showed dual properties of thermo- and pH-responsiveness in an aqueous solution. Ultraviolet-visible spectroscopy and dynamic light scattering were employed to study the phase behavior under varying temperatures and pH values. Unlike the phase transition temperatures of other graft copolymers containing non-ionic blocks, the phase transition temperature of these polymers was easily tuned by changing the polymer concentration. Owing to the biocompatible and stimuli-responsive nature of the polymers, this system was shown to effectively release proteins (lysozyme) while simultaneously protecting them against denaturation. The positively charged lysozyme was shown to bind with the negatively charged polymer at the physiological pH (pH 7.4). However, it was subsequently released at pH 3, at which the polymer exhibits a positive charge. Protein aggregation studies using a residual enzymatic activity assay, circular dichroism, and a Thioflavin T assay revealed that the secondary structure of the lysozyme was retained even after harsh thermal treatment. The addition of these polymers helped the lysozyme retain its enzymatic activity and suppressed its fibrillation. Both polymers showed excellent protein protection properties, with the negatively charged polymer exhibiting slightly superior protein protection properties to those of the neutral polymer. To the best of the authors’ knowledge, this is the first study to develop a graft copolymer system consisting of two different zwitterionic blocks that shows dual thermo- and pH-responsive properties. The presence of the polyampholyte structure enables these polymers to act as protein release agents, while simultaneously protecting the proteins from severe stress.
- Subjects :
- Circular dichroism
Hot Temperature
Materials science
Polymers
02 engineering and technology
Protein aggregation
010402 general chemistry
polyampholyte
01 natural sciences
Cell Line
Polymerization
protein aggregation
Mice
Protein Aggregates
Dynamic light scattering
Copolymer
Animals
General Materials Science
Denaturation (biochemistry)
chemistry.chemical_classification
dual thermo-responsive
protein release
Chain transfer
Polymer
Hydrogen-Ion Concentration
021001 nanoscience & nanotechnology
0104 chemical sciences
pH responsive
chemistry
Chemical engineering
Muramidase
0210 nano-technology
Subjects
Details
- ISSN :
- 19448252 and 19448244
- Volume :
- 11
- Database :
- OpenAIRE
- Journal :
- ACS Applied Materials & Interfaces
- Accession number :
- edsair.doi.dedup.....e245d3eaf4bd1341760847ddc002b9e9