Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin

Foo, Yiing Yee; Kabir, Md. Zahirul; Periasamy, Vengadesh; Malek, Sri Nurestri Abd; Tayyab, Saad

doi:10.1016/j.molliq.2018.05.115

Cited by 15 publications

(12 citation statements)

References 48 publications

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“…This would result in a decrease in the fluorescence quenching (Ksv and kq) and an increase in the fluorescence yield [73], which is different from our results. This result is in agreement with the dynamic quenching of HSA by AuNPs reported by Foo et al and Yin et al [74,75].…”

Section: Fluorescence Spectroscopysupporting

confidence: 93%

Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

Yang

Bolsa-Ferruz

Marichal

et al. 2020

IJMS

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The gadolinium-based nanoagent named AGuIX® is a unique radiosensitizer and contrast agent which improves the performance of radiotherapy and medical imaging. Currently tested in clinical trials, AGuIX® is administrated to patients via intravenous injection. The presence of nanoparticles in the blood stream may induce harmful effects due to undesired interactions with blood components. Thus, there is an emerging need to understand the impact of these nanoagents when meeting blood proteins. In this work, the influence of nanoagents on the structure and stability of the most abundant blood protein, human serum albumin, is presented. Synchrotron radiation circular dichroism showed that AGuIX® does not bind to the protein, even at the high ratio of 45 nanoparticles per protein at 3 mg/L. However, it increases the stability of the albumin. Isothermal thermodynamic calorimetry and fluorescence emission spectroscopy demonstrated that the effect is due to preferential hydration processes. Thus, this study confirms that intravenous injection of AGuIX® presents limited risks of perturbing the blood stream. In a wider view, the methodology developed in this work may be applied to rapidly evaluate the impact and risk of other nano-products that could come into contact with the bloodstream.

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Section: Fluorescence Spectroscopysupporting

confidence: 93%

Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

Yang

Bolsa-Ferruz

Marichal

et al. 2020

IJMS

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“…Our docking results supported this view, showing involvement of hydrogen bonds in the complex formation (Table ). Several published reports have shown the involvement of hydrophobic interactions and hydrogen bonds based on the thermodynamic data and docking analyses . It is imperative to believe structural alterations in the protein consequent to ligand binding.…”

Section: Discussionmentioning

confidence: 99%

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

et al. 2019

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The interaction between mefloquine (MEF), the antimalarial drug, and human serum albumin (HSA), the main carrier protein in blood circulation, was explored using fluorescence, absorption, and circular dichroism spectroscopic techniques. Quenching of HSA fluorescence with MEF was characterized as static quenching and thus confirmed the complex formation between MEF and HSA. Association constant values for MEF‐HSA interaction were found to fall within the range of 3.79‐5.73 × 104 M˗1 at various temperatures (288, 298, and 308 K), which revealed moderate binding affinity. Hydrogen bonds and hydrophobic interactions were predicted to connect MEF and HSA together in the MEF‐HSA complex, as deduced from the thermodynamic data (ΔS = +133.52 J mol−1 K−1 and ΔH = +13.09 kJ mol−1) of the binding reaction and molecular docking analysis. Three‐dimensional fluorescence spectral analysis pointed out alterations in the microenvironment around aromatic amino acid (tryptophan and tyrosine) residues of HSA consequent to the addition of MEF. Circular dichroic spectra of HSA in the wavelength ranges of 200‐250 and 250‐300 nm hinted smaller changes in the protein's secondary and tertiary structures, respectively, induced by MEF binding. Noncovalent conjugation of MEF to HSA bettered protein thermostability. Site marker competitive drug displacement results suggested HSA Sudlow's site I as the MEF binding site, which was also supported by molecular docking analysis.

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“…Ultraviolet‐visible (UV‐VIS) spectroscopy is one of the quite common methods for the characterization of the localized surface plasmon resonance (LSPR) of GNPs . LSPR refers to the phenomenon of resonant oscillation of conduction electrons on a metal surface induced by incident light.…”

Section: Characterization Of Functionalized Gnpsmentioning

confidence: 99%

Functionalized gold nanoparticles for sample preparation: A review

Liu

Lämmerhofer

2019

Electrophoresis

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Sample preparation is a crucial step for the reliable and accurate analysis of both small molecule and biopolymers which often involves processes such as isolation, pre‐concentration, removal of interferences (purification), and pre‐processing (e.g., enzymatic digestion) of targets from a complex matrix. Gold nanoparticle (GNP)‐assisted sample preparation and pre‐concentration has been extensively applied in many analytical procedures in recent years due to the favorable and unique properties of GNPs such as size‐controlled synthesis, large surface‐to‐volume ratio, surface inertness, straightforward surface modification, easy separation requiring minimal manipulation of samples. This review article primarily focuses on applications of GNPs in sample preparation, in particular for bioaffinity capture and biocatalysis. In addition, their most common synthesis, surface modification and characterization methods are briefly summarized. Proper surface modification for GNPs designed in accordance to their target application directly influence their functionalities, e.g., extraction efficiencies, and catalytic efficiencies. Characterization of GNPs after synthesis and modification is worthwhile for monitoring and controlling the fabrication process to ensure proper quality and functionality. Parameters such as morphology, colloidal stability, and physical/chemical properties can be assessed by methods such as surface plasmon resonance, dynamic light scattering, ζ‐potential determinations, transmission electron microscopy, Taylor dispersion analysis, and resonant mass measurement, among others. The accurate determination of the surface coverage appears to be also mandatory for the quality control of functionality of the nanoparticles. Some promising applications of (functionalized) GNPs for bioanalysis and sample preparation are described herein.

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Spectroscopic studies on the interaction of green synthesized-gold nanoparticles with human serum albumin

Cited by 15 publications

References 48 publications

Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

Human Serum Albumin in the Presence of AGuIX Nanoagents: Structure Stabilisation without Direct Interaction

Combination mode of antimalarial drug mefloquine and human serum albumin: Insights from spectroscopic and docking approaches

Functionalized gold nanoparticles for sample preparation: A review

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