In-situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA

Iranpour Anaraki, Neda; Liebi, Marianne; Ong, Quy; Blanchet, Clément; Maurya, Anjani K.; Stellacci, Francesco; Salentinig, Stefan; Wick, Peter; Neels, Antonia

doi:10.1002/adfm.202110253

Title: In-situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA

Journal Article · Sun Nov 21 00:00:00 EST 2021 · Advanced Functional Materials

DOI:https://doi.org/10.1002/adfm.202110253· OSTI ID:1889832

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Swiss Federal Laboratories for Materials Science and Technology, St. Gallen (Switzerland); University of Fribourg (Switzerland)
Swiss Federal Laboratories for Materials Science and Technology, St. Gallen (Switzerland); Chalmers University of Technology, Gothenburg (Sweden)
Ecole Polytechnique Federale Lausanne (EPFL) (Switzerland)
European Molecular Biology Laboratory, Hamburg (Germany)
Swiss Federal Laboratories for Materials Science and Technology, St. Gallen (Switzerland); SLAC National Accelerator Lab., Menlo Park, CA (United States). Stanford Synchrotron Radiation Lightsource (SSRL)
University of Fribourg (Switzerland)
Swiss Federal Laboratories for Materials Science and Technology, St. Gallen (Switzerland)

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.

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Research Organization:: SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)

Sponsoring Organization:: USDOE Office of Science (SC); Swiss National Science Foundation (SNSF); Competence Centre for Materials Science and Technology (CCMX)

Grant/Contract Number:: AC02-76SF00515; 200020_185062

OSTI ID:: 1889832

Journal Information:: Advanced Functional Materials, Vol. 32, Issue 9; ISSN 1616-301X

Publisher:: WileyCopyright Statement

Country of Publication:: United States

Language:: English

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36 MATERIALS SCIENCE
aggregation
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human serum albumin
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small-angle X-ray scattering
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Title: In-situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA

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