Topology-Dependent Interaction of Cyclic Poly(ethylene glycol) Complexed with Gold Nanoparticles against Bovine Serum Albumin for a Colorimetric Change
Unique physical and chemical properties arising from a polymer topology recently draw significant attention. In this study, cyclic poly(ethylene glycol) (c-PEG) was found to significantly interact with bovine serum albumin (BSA), suggested by nuclear magnetic resonance, dynamic light scattering, and...
Veröffentlicht in: | Langmuir : the ACS journal of surfaces and colloids. - 1992. - 38(2022), 17 vom: 03. Mai, Seite 5286-5295 |
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Weitere Verfasser: | , , , , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2022
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Zugriff auf das übergeordnete Werk: | Langmuir : the ACS journal of surfaces and colloids |
Schlagworte: | Journal Article Serum Albumin, Bovine 27432CM55Q Polyethylene Glycols 3WJQ0SDW1A Gold 7440-57-5 |
Zusammenfassung: | Unique physical and chemical properties arising from a polymer topology recently draw significant attention. In this study, cyclic poly(ethylene glycol) (c-PEG) was found to significantly interact with bovine serum albumin (BSA), suggested by nuclear magnetic resonance, dynamic light scattering, and fluorescence spectroscopy. On the other hand, linear HO-PEG-OH and MeO-PEG-OMe showed no affinity. Furthermore, a complex of gold nanoparticles and c-PEG (AuNPs/c-PEG) attracted BSA to form aggregates, and the red color of the AuNPs dispersion evidently disappeared, whereas ones with linear PEG or without PEG did not demonstrate such a phenomenon. The interactions among BSA, AuNPs, and PEG were investigated by changing the incubation time and concentration of the components by using UV-Vis and fluorescence spectroscopy |
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Beschreibung: | Date Completed 04.05.2022 Date Revised 04.05.2022 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1520-5827 |
DOI: | 10.1021/acs.langmuir.1c03027 |