Photochemical Consideration in the Interactions between Blood Proteins and Layered Inorganic Materialsopen access
- Authors
- Yamaguchi, Tetsuo; Kim, Hyoung-Mi; Oh, Jae-Min
- Issue Date
- Oct-2022
- Publisher
- MDPI
- Keywords
- layered double hydroxide; human serum albumin; gamma-globulin; fibrinogen; biocompatibility; fluorescence quenching
- Citation
- International Journal of Molecular Sciences, v.23, no.19, pp 1 - 13
- Pages
- 13
- Indexed
- SCIE
SCOPUS
- Journal Title
- International Journal of Molecular Sciences
- Volume
- 23
- Number
- 19
- Start Page
- 1
- End Page
- 13
- URI
- https://scholarworks.dongguk.edu/handle/sw.dongguk/2482
- DOI
- 10.3390/ijms231911367
- ISSN
- 1661-6596
1422-0067
- Abstract
- Interactions between layered double hydroxide (LDH) nanomaterials and plasma proteins according to their particle size and surface charge were evaluated. The LDHs with different particle size (150, 350 and 2000 nm) were prepared by adjusting hydrothermal treatment and urea hydrolysis and subsequent organic coating with citrate, malite and serite was applied to control the surface charge (zeta-potential: -15, 6 and 36 mV). Adsorption isotherms and Stern-Volmer plots for fluorescence quenching indicated that the human blood plasma had weak interactions toward all the types of LDHs. The adsorption isotherms did not show significant differences in the size and surface charges, while the fluorescence quenching ratio increased with the increase in the surface charge, implying that electrostatic interaction played a major role in their interactions. The fluorescence quenching of three types of plasma proteins (human serum albumin, gamma-globulin and fibrinogen) by the surface charge-controlled LDHs suggested that the proteins adsorbed on the LDHs with a single layer and additional proteins were weakly adsorbed to surround the LDHs with adsorbed proteins. It was concluded that the LDH nanomaterials are fairly compatible for blood components due to the protein corona while the electrostatic interaction can affect their interaction with the proteins.
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Collections - College of Engineering > Department of Energy and Materials Engineering > 1. Journal Articles

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