In‐situ Investigations on Gold Nanoparticles Stabilization Mechanisms in Biological Environments Containing HSA. (21st November 2021)

• Record Type: Journal Article
• Authors: Iranpour Anaraki, Neda; Liebi, Marianne; Ong, Quy; Blanchet, Clément; Maurya, Anjani K.; Stellacci, Francesco; Salentinig, Stefan; Wick, Peter; Neels, Antonia
• Is Part Of: Advanced functional materials. Volume 32:Number 9(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2021-11-21
• Subjects: aggregation -- colloidal stability -- gold nanoparticles -- human serum albumin -- protein corona -- small‐angle X‐ray scattering -- UV–visible spectroscopy; Materials -- Periodicals; Chemical vapor deposition -- Periodicals; 620.11
• DOI: 10.1002/adfm.202110253
• Languages: English
• ISSNs: 1616-301X

Abstract

Abstract: 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. Abstract : The effect of nanoparticle (NP) size and surface modification on colloidal stability in NaCl and protein solutions is studied. Two significantly different stabilization mechanisms have been investigated in detail for citrate‐capped and PEGylated gold NPs. Citrate‐capped NPs stabilize by protein adsorption on their surfaces while PEGylated NPs build a self‐assembled ordered 3D arrangement, resulting in a long‐term colloid stabilization.