Adsorption of Human Serum Albumin on Graphene Oxide: Implications for Protein Corona Formation and Conformation
| Autor: | Kai Loon Chen, Xitong Liu, Chenxu Yan |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Surface Properties
Protein Corona Serum Albumin Human 010501 environmental sciences Photochemistry 01 natural sciences Adsorption medicine Environmental Chemistry Humans Lipid bilayer 0105 earth and related environmental sciences Chemistry Oxides General Chemistry Quartz crystal microbalance Human serum albumin body regions Membrane Isoelectric point Ionic strength embryonic structures Quartz Crystal Microbalance Techniques Graphite medicine.drug |
| Zdroj: | Environmental sciencetechnology. 53(15) |
| ISSN: | 1520-5851 |
| Popis: | The influence of solution chemistry on the adsorption of human serum albumin (HSA) proteins on graphene oxide (GO) was investigated through batch adsorption experiments and the use of a quartz crystal microbalance with dissipation (QCM-D). The conformation of HSA layers on GO was also examined with the QCM-D. Our results show that an increase in ionic strength under neutral pH conditions resulted in stronger binding between HSA and GO, as well as more compact HSA layers on GO, emphasizing the key role of electrostatic interactions in controlling HSA-GO interactions. Calcium ions also facilitated HSA adsorption likely through charge neutralization and bridging effect. At physiological ionic strength conditions (150 mM), maximum HSA adsorption was observed at the isoelectric point of HSA (4.7). Under acidic conditions, the adsorption of HSA on GO led to the formation of protein layers with a high degree of fluidity due to the extended conformation of HSA. Finally, the attachment of GO to a supported lipid bilayer that was composed of zwitterionic 1,2-dioleoyl-sn-glycero-3-phosphocholine, a model for cell membranes, was reduced in the presence of protein coronas. This reduction in GO attachment was influenced by the conformation of the protein coronas on GO. |
| Databáze: | OpenAIRE |
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