In‐situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA
Autor: | Marianne Liebi, Quy Khac Ong, Antonia Neels, Francesco Stellacci, Anjani K. Maurya, Clément Blanchet, Neda Iranpour Anaraki, Peter Wick, Stefan Salentinig |
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Rok vydání: | 2021 |
Předmět: |
In situ
Materials science Protein Corona Photochemistry Biomaterials protein corona Ultraviolet visible spectroscopy small-angle x-ray scattering Electrochemistry medicine ddc:530 colloidal stability uv-visible spectroscopy thermodynamic properties Small-angle X-ray scattering exchange aggregation technology industry and agriculture Condensed Matter Physics Human serum albumin particle-size Electronic Optical and Magnetic Materials human serum albumin adsorption Colloidal gold gold nanoparticles impact acid medicine.drug |
Zdroj: | Advanced functional materials 32(9), 2110253-(2022). doi:10.1002/adfm.202110253 |
ISSN: | 1616-3028 1616-301X |
Popis: | Advanced functional materials 32(9), 2110253 - (2022). doi:10.1002/adfm.202110253 Nanoparticles (NPs) developments advance innovative biomedical applications. However, complex interactions and the low colloidal stability of NPs in biological media restrict their widespread utilization. The influence of NPs properties on the colloidal stability for gold NPs with 5 and 40 nm in diameter with two surface modifications, methoxy-polyethylene glycol-sulfhydryl (PEG) and citrate, in NaCl and human serum albumin (HSA) protein solution, is investigated. This study is based on small-angle X-ray scattering (SAXS) methods allowing the in-situ monitoring of interactions in physiological conditions. The PEG coating provides high colloidal stability for NPs of both sizes. For 5 nm NPs in NaCl solution, a stable 3D self-assembled body-centered cubic (BCC) arrangement is detected with an interparticle distance of 20.7 ± 0.1 nm. In protein solution, this distance increases to 21.9 ± 0.1 nm by protein penetration inside the ordered structure. For citrate-capped NPs, a different mechanism is observed. The protein particles attach to the NPs surfaces, and an appropriate concentration of proteins results in a stable suspension. Cryogenic transmission electron microscopy (Cryo-TEM), UV–visible spectroscopy, and dynamic light scattering (DLS) support the SAXS results. The findings will pave the way to design and synthesize NPs with controlled behaviors in biomedical applications. Published by Wiley-VCH, Weinheim |
Databáze: | OpenAIRE |
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