Thin Film Formation of HSA in the Presence of CTAB-Capped Gold Nanorods through Phase Separation.

IF 3.7 2区 化学 Q2 CHEMISTRY, MULTIDISCIPLINARY
Langmuir Pub Date : 2024-07-23 Epub Date: 2024-07-02 DOI:10.1021/acs.langmuir.4c00694
Krishna Halder, Kabira Sabnam, Abhirup Das, Dipak K Goswami, Swagata Dasgupta
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引用次数: 0

Abstract

Phase behavior in protein-nanoparticle systems in light of protein corona formation has been investigated. We report the formation of HSA thin films following the addition of a solid protein to a solution of CTAB-capped gold nanorods (AuNRs) via phase separation. The phase separation behavior was observed through UV-vis spectroscopy, turbidity assays, and DLS studies. UV-vis spectra for the protein-AuNR solution indicated a possible self-assembly formation by CTAB-HSA complexes and AuNR-HSA conjugates. The turbidity was found to increase linearly up to 30-50% v/v for each component. The growth phase slope is proportional to the concentration of the components, AuNRs, and HSA, with no lag phase. Dynamic light scattering (DLS) shows the formation of larger aggregates with time, implying a segregated phase of AuNR-HSA and a CTAB-HSA-AuNR network. ζ-potential values confirm surface modification, implying protein corona formation on nanorods. The thin films were also characterized using SEM, AFM, SAXS, XPS, FTIR, and TGA studies. SEM images show a smooth surface with a reduced number of pores, indicating the compactness of the deposited structure. AFM shows two different structural pattern formations with the deposition, indicating possible self-assembly of the protein-conjugated nanoparticles. FTIR studies indicate a change in the hydrogen bonding network and confirm the CTAB-HSA-AuNR complex network formation. The XPS studies indicate Au-S bond formation, along with Au-S-S-Au interactions. SAXS studies indicate the formation of aggregates (oligomers), as well as the presence of dominant attractive intermolecular interactions in the thin films.

Abstract Image

通过相分离在 CTAB 封装的金纳米棒中形成 HSA 薄膜。
鉴于蛋白质电晕的形成,我们对蛋白质-纳米粒子系统中的相行为进行了研究。我们报告了在 CTAB 封顶金纳米棒(AuNRs)溶液中加入固体蛋白质后通过相分离形成 HSA 薄膜的情况。我们通过紫外-可见光谱、浊度测定和 DLS 研究观察了相分离行为。蛋白质-AuNR 溶液的紫外-可见光谱表明,CTAB-HSA 复合物和 AuNR-HSA 共轭物可能形成了自组装。研究发现,每种成分的浊度在达到 30-50% v/v 时都会线性增加。生长阶段的斜率与成分、AuNR 和 HSA 的浓度成正比,没有滞后阶段。动态光散射(DLS)显示,随着时间的推移会形成更大的聚集体,这意味着 AuNR-HSA 和 CTAB-HSA-AuNR 网络处于分离阶段。ζ-电位值证实了表面改性,意味着在纳米棒上形成了蛋白质电晕。此外,还使用 SEM、AFM、SAXS、XPS、FTIR 和 TGA 研究对薄膜进行了表征。扫描电镜图像显示薄膜表面光滑,孔隙数量减少,表明沉积结构紧密。原子力显微镜显示沉积过程中形成了两种不同的结构模式,表明蛋白质共轭纳米粒子可能是自组装的。傅立叶变换红外光谱研究表明氢键网络发生了变化,证实了 CTAB-HSA-AuNR 复合物网络的形成。XPS 研究表明形成了 Au-S 键以及 Au-S-S-Au 相互作用。SAXS 研究表明在薄膜中形成了聚集体(低聚物),并存在主要的分子间吸引力相互作用。
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来源期刊
Langmuir
Langmuir 化学-材料科学:综合
CiteScore
6.50
自引率
10.30%
发文量
1464
审稿时长
2.1 months
期刊介绍: Langmuir is an interdisciplinary journal publishing articles in the following subject categories: Colloids: surfactants and self-assembly, dispersions, emulsions, foams Interfaces: adsorption, reactions, films, forces Biological Interfaces: biocolloids, biomolecular and biomimetic materials Materials: nano- and mesostructured materials, polymers, gels, liquid crystals Electrochemistry: interfacial charge transfer, charge transport, electrocatalysis, electrokinetic phenomena, bioelectrochemistry Devices and Applications: sensors, fluidics, patterning, catalysis, photonic crystals However, when high-impact, original work is submitted that does not fit within the above categories, decisions to accept or decline such papers will be based on one criteria: What Would Irving Do? Langmuir ranks #2 in citations out of 136 journals in the category of Physical Chemistry with 113,157 total citations. The journal received an Impact Factor of 4.384*. This journal is also indexed in the categories of Materials Science (ranked #1) and Multidisciplinary Chemistry (ranked #5).
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