Temperature Dependent and Kinetic Study of the Adsorption of Bovine Serum Albumin to ZnO Nanoparticle Surfaces

Bhunia, Amit Kumar; Kamilya, Tapanendu; Saha, Suman

doi:10.1002/slct.201600446

Cited by 26 publications

(17 citation statements)

References 75 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Similar results were observed in the articles which the ground state complex between proteins 138 and NPs was formed [25,27] . Therefore, this increasing in the absorption intensity can be due to 139 formation of the ground state complex between HSA and ZnO NPs.…”

supporting

confidence: 89%

See 1 more Smart Citation

Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

Hassanian

Aryapour

Goudarzi

et al. 2018

Preprint

View full text Add to dashboard Cite

8With due attention to adsorption of proteins on the nanoparticles surface and the formation of 9 nanoparticle-protein corona, investigation of nanoparticles toxicity on the structure of proteins is 10 important. Therefore, this work was done to evaluate toxicity of Zinc oxide nanoparticles (ZnO 11 NPs) on the structure of human serum albumin (HSA) through in vitro and in silico studies. First, 12 ZnO NPs were synthesized using hydrothermal method and their size and morphology were 13 determined by SEM and TEM methods and then to study its toxicity on the HSA structure were 14 used UV-Vis and fluorescence spectroscopy. Also, in order to investigate interaction mechanism 15 of ZnO NP with HSA at the atomistic level was used molecular dynamics (md) simulation. The 16 obtained images from SEM and TEM showed that ZnO NPs were nanosheet with size of less 17 than 40 nm. The results of spectroscopic studies showed ZnO NPs lead to significant 18 conformational changes in the protein's absorption and emission spectra. Moreover, md results 19 showed the minor structure changes in HSA due to interaction with ZnO NP during the 100 ns 20 simulation and the formation of nanoparticle-protein corona complex that is mainly because of 21 electrostatic interactions between charge groups of HSA and ZnO NP. 22Toxicity 24 25 human body, they may interact with biomacromolecules and even biological metabolites due to 32 their nano size and large surface to mass ratio. But, the adsorption of proteins on the surface of 33 NPs and the formation of nanoparticle-protein complex which is known as the nanoparticle-34 protein corona (NP-PC), is unique [2] . On the other hand, adsorption of proteins on the NPs 35 surface may result in structural changes and unfolding of proteins and lead to toxicity [3] . The 36 previous studies showed that the binding of ZnO NPs led to the denaturation of the periplasmic 37 domain of ToxR protein of Vibrio cholerae [4] . Therefore, it is important to study the toxicity of 38 NPs on the structure of proteins to design nanoparticle that do not have toxic effects on the 39 structure of proteins and consequently, on living organisms. In this study, we synthesized ZnO 40 NPs and studied their toxicity on human serum albumin (HSA). These nanoparticles are an 41 important class of commercially applied material and used in diagnostics, therapeutics, drug 42 delivery systems, electronics, cosmetics, personal care products, food additives and pigments and 43 coatings due to their magnetic, catalytic, semiconducting, antimicrobial, ultraviolet protective 44 and binding properties [5] . Moreover, human serum albumin is the most abundant type of plasma 45 protein (3.5 to 5.5 g/dL) with highest electrophoretic mobility, and it has a globular structure 46 with a molecular weight 66.5 kDa, consists of 585 amino acids, 17 disulfide bonds, and only one 47 100 2018 [15] . The crystallographic structure of human serum albumin (PDB ID: 1e7e) was obtained 101 from Protein Data Bank [16] . To understand the mechanism of ZnO NP...

show abstract

supporting

confidence: 89%

“…Nanotechnology is the ability to study and use of particles in dimensions between 1-100 nm 27 which commonly known as nanoparticles (NPs). NPs have unique mechanical and chemical 28 properties arising from their high surface area and quantum effects.…”

mentioning

confidence: 99%

Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

Hassanian

Aryapour

Goudarzi

et al. 2018

Preprint

View full text Add to dashboard Cite

show abstract

“…The relative kinetic efficiency of fluorescence quenching can be determined by fitting the dependence of F o/F on PbS NP concentration (Figure D) based on a fitting to the Stern‐Volmer equation . Equation

true \frac{F^{0}}{F} = 1 + K_{s v} ([], N, P)

…”

Section: Resultsmentioning

confidence: 99%

“…The energy transfer efficiency between nanoparticles and protein is measured using the relative emission intensity of the protein, in the absence (I 0 ) and the presence (I) of nanoparticles Equation

true Q_{normale normalf normalf} = 1 - \frac{I}{{normalI}_{0}}

…”

Section: Resultsmentioning

confidence: 99%

Photo Relaxation Change and Emission Quenching in Different Sizes of PbS‐Nanoparticles‐Protein Corona

Bhunia

Kamilya²,

Saha

2016

ChemistrySelect

Self Cite

View full text Add to dashboard Cite

In this study, energy transfer from BSA to different size semiconductor nanoparticles PbS was analyzed by using photo Relaxation change and emission quenching analysis. Structures of thePbS NPs are studied by XRD, TEM, and FT-IR measurements. The band gap and crystal size of PbS suggest the quantum confinement effect. Photo current of the BSA-PbS NPs bioconjugate system increased compared to bare PbS nanoparticles from nA to mA. Change in photo relaxation life time of the bare PbS NP and PbS NPs-BSA bioconjugate system is particle size dependent and interaction dependent. PbS NPs-BSA bioconjugate were characterized by steady-state fluorescence spectroscopy to determine the magnitude and mechanism of the energy transfer. It was found that the BSA fluorescence was quenched after the addition of PbS nanoparticles. Quenching of protein is large for larger size PbS nanoparticles. DLS study confirmed that BSA was adsorbed onto the surface of nanoparticles, creating a favourable geometry for quenching. Aggregation of BSA around a single PbS nanoparticle is size dependent. Larger nanoparticles are responsible for hard as well as soft corona due to interaction.-Our results, which include photo relaxation times, energy transfer efficiencies showed that energy transferred take place via the Fluorescence Resonance Energy Transfer (FRET) mechanism. These energy transfer processes between protein molecules and PbS nanoparticles, will depend on the size of the particles involved.

show abstract

“…Before using various applications, it is substantially essential to grasp the manner of interaction of bare ZnO NPs with blood proteins. In our previous publications, we reported the interaction and bioconjugate formation of ZnO NPs with the model protein bovine serum albumin (BSA). Whenever NPs are available to contact physiological fluid systems they are encircled by the biological molecules such as protein, lipid, or enzymes .…”

Section: Introductionmentioning

confidence: 99%

Microscopic and spectroscopic study of the corona formation and unfolding of human haemoglobin in presence of ZnO nanoparticles

Bhunia

Saha

Kamilya³

2019

Luminescence

View full text Add to dashboard Cite

The interaction of zinc oxide nanoparticles (ZnO NPs) with human haemoglobin (Hb) is studied for the biologically safe application of ZnO NPs in the human body. The Hb corona is formed around the ZnO nanoparticles, directly observed from highresolution transmission electron microscopy (HRTEM) images. Hb formed 'hard corona' on the surface of ZnO NPs from an exponential association mechanism over a very short duration, as well as unfolding of Hb that occurred over a long lifetime.Dynamic light scattering measurements demonstrated that the ZnO NPs were completely covered by Hb with shell thickness of c. 6 nm that formed a 'hard corona'.Zeta potential measurements represented that the ZnO NPs were fully covered by Hb molecules using an exponential association mechanism. Tryptophans (TRY), as well as heme-porphyrin moieties of Hb, are the major binding sites for ZnO NPs.The nature of the interaction between ZnO NPs and Hb was analysed from the fluorescence quenching of TRYs. Electrostatic interaction, along with the hydrophobic interaction between ZnO NPs and Hb, is responsible for the conformational change in Hb due to increase in the percentage of β-sheets together with a decrease in αhelices.

show abstract

Temperature Dependent and Kinetic Study of the Adsorption of Bovine Serum Albumin to ZnO Nanoparticle Surfaces

Cited by 26 publications

References 75 publications

Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

Are Zinc oxide nanoparticles safe? A structural study on human serum albumin using in vitro and in silico methods

Photo Relaxation Change and Emission Quenching in Different Sizes of PbS‐Nanoparticles‐Protein Corona

Microscopic and spectroscopic study of the corona formation and unfolding of human haemoglobin in presence of ZnO nanoparticles

Contact Info

Product

Resources

About