Synchrotron radiation circular dichroism spectroscopy reveals that gold and silver nanoparticles modify the secondary structure of a lung surfactant protein B analogue

Buckley, Alison; Warren, James A.; Hussain, Rohanah; Smith, Rachel

doi:10.1039/d2nr06107d

Cited by 7 publications

(5 citation statements)

References 76 publications

(105 reference statements)

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“…It is effective in the case of studying protein interactions with nanoparticles. Our colleagues have shown [ 33 ] that the size and concentration of nanoparticles affect the peptide conformation, in particular, reducing the number of α-helices and increasing the number of β-sheets. In our study, at pH 3.9 and 7.5, on the contrary, there is an increase in α-helices and a decrease in the number of β-sheets.…”

Section: Discussionmentioning

confidence: 99%

pH-Dependent HEWL-AuNPs Interactions: Optical Study

Molkova,

Pustovoy,

Stepanova

et al. 2023

Molecules

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Optical methods (spectroscopy, spectrofluorometry, dynamic light scattering, and refractometry) were used to study the change in the state of hen egg-white lysozyme (HEWL), protein molecules, and gold nanoparticles (AuNPs) in aqueous colloids with changes in pH, and the interaction of protein molecules with nanoparticles was also studied. It was shown that changing pH may be the easiest way to control the protein corona on gold nanoparticles. In a colloid of nanoparticles, both in the presence and absence of protein, aggregation–deaggregation, and in a protein colloid, monomerization–dimerization–aggregation are the main processes when pH is changed. A specific point at pH 7.5, where a transition of the colloidal system from one state to another is observed, has been found using all the optical methods mentioned. It has been shown that gold nanoparticles can stabilize HEWL protein molecules at alkaline pH while maintaining enzymatic activity, which can be used in practice. The data obtained in this manuscript allow for the state of HEWL colloids and gold nanoparticles to be monitored using one or two simple and accessible optical methods.

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Section: Discussionmentioning

confidence: 99%

pH-Dependent HEWL-AuNPs Interactions: Optical Study

Molkova,

Pustovoy,

Stepanova

et al. 2023

Molecules

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“…In addition, SRCD was used to demonstrated that Au and Ag nanoparticles can cause conformational changes in the structure of a key component of surfactant protein B, which plays a key role in the biophysical function of lung surfactant and is essential to life, which could change its effect in vivo, potentially leading to alterations in lung surfactant function and ultimately the physiological behavior of the lung [70]. In this case, most of the spectral change occurs bellow 210 nm.…”

Section: Synchrotron Radiation Circular Dichroism (Srcd) Spectroscopymentioning

confidence: 99%

Unlocking Insights into Folding, Structure, and Function of Proteins through Circular Dichroism Spectroscopy—A Short Review

Linhares,

Ramos

2023

Applied Biosciences

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Circular dichroism (CD) spectroscopy has emerged as a powerful tool in the study of protein folding, structure, and function. This review explores the versatile applications of CD spectroscopy in unraveling the intricate relationship between protein conformation and biological activity. A key advantage of CD spectroscopy is its ability to analyze protein samples with minimal quantity requirements, making it an attractive technique for studying proteins that are scarce or difficult to produce. Moreover, CD spectroscopy enables the monitoring of physical and chemical environmental effects on protein structures, providing valuable insights into the dynamic behavior of proteins in different conditions. In recent years, the use of synchrotron radiation as a light source for CD measurements has gained traction, offering enhanced sensitivity and resolution. By combining the advantages of CD spectroscopy, such as minimal sample requirements and the ability to probe environmental effects, with the emerging capabilities of synchrotron radiation (SRCD), researchers have an unprecedented opportunity to explore the diverse aspects of protein behavior. This review highlights the significance of CD spectroscopy in protein research and the growing role of synchrotron radiation in advancing our understanding of protein behavior, aiming to provide novel insights and applications in various fields, including drug discovery, protein engineering, and biotechnology. A brief overview of Solid-State Circular Dichroism (SSCD) is also included.

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“…The formation of PCs is a complex process that is influenced by the properties of the protein (protein charge, hydrophobicity, size, conformation) and by the properties of the nanomaterial (nanoparticle size, shape, functionalization) . Numerous advances in experimental techniques have led to a better understanding of the influence of some of these factors on PC formation. − Among the characterization techniques employed, some rely on changes in size and surface charge during the formation of the PC including dynamic light scattering (DLS), fluorescence correlation spectroscopy (FCS), − UV–visible spectroscopy, , and gel electrophoresis. , In addition, mass spectrometry (MS), , circular dichroism (CD), , and Fourier transform infrared spectroscopy (FT-IR) , enabled the identification and quantification of proteins in the corona. However, as most techniques are not in situ, they result in long processing times, molecular biases in purification processes, and loss of single-particle information.…”

mentioning

confidence: 99%

“…12−16 Among the characterization techniques employed, some rely on changes in size and surface charge during the formation of the PC including dynamic light scattering (DLS), 17 (FCS), 18−20 UV−visible spectroscopy, 21,22 and gel electrophoresis. 23,24 In addition, mass spectrometry (MS), 25,26 circular dichroism (CD), 27,28 and Fourier transform infrared spectroscopy (FT-IR) 29,30 enabled the identification and quantification of proteins in the corona. However, as most techniques are not in situ, they result in long processing times, molecular biases in purification processes, and loss of singleparticle information.…”

mentioning

confidence: 99%

Real-Time Optical Tracking of Protein Corona Formation on Single Nanoparticles in Serum

Dolci,

Wang,

Nooteboom

et al. 2023

ACS Nano

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The formation of a protein corona, where proteins spontaneously adhere to the surface of nanomaterials in biological environments, leads to changes in their physicochemical properties and subsequently affects their intended biomedical functionalities. Most current methods to study protein corona formation are ensemble-averaging and either require fluorescent labeling, washing steps, or are only applicable to specific types of particles. Here we introduce real-time all-optical nanoparticle analysis by scattering microscopy (RONAS) to track the formation of protein corona in full serum, at the single-particle level, without any labeling. RONAS uses optical scattering microscopy and enables real-time and in situ tracking of protein adsorption on metallic and dielectric nanoparticles with different geometries directly in blood serum. We analyzed the adsorbed protein mass, the affinity, and the kinetics of the protein adsorption at the single particle level. While there is a high degree of heterogeneity from particle to particle, the predominant factor in protein adsorption is surface chemistry rather than the underlying nanoparticle material or size. RONAS offers an in-depth understanding of the mechanisms related to protein coronas and, thus, enables the development of strategies to engineer efficient bionanomaterials.

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Synchrotron radiation circular dichroism spectroscopy reveals that gold and silver nanoparticles modify the secondary structure of a lung surfactant protein B analogue

Abstract: Synchrotron radiation circular dichroism shows that gold and silver nanoparticles modify the secondary structure of lung surfactant protein-B analogue SP-B1–25.

Cited by 7 publications

References 76 publications

pH-Dependent HEWL-AuNPs Interactions: Optical Study

pH-Dependent HEWL-AuNPs Interactions: Optical Study

Unlocking Insights into Folding, Structure, and Function of Proteins through Circular Dichroism Spectroscopy—A Short Review

Real-Time Optical Tracking of Protein Corona Formation on Single Nanoparticles in Serum

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