Spectroscopic and coarse-grained simulation studies of the BSA and HSA protein adsorption on silver nanoparticles

Voicescu, Mariana; Ionescu, Sorana; Angelescu, Daniel G.

doi:10.1007/s11051-012-1174-0

Cited by 48 publications

(25 citation statements)

References 65 publications

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“…2. Similar results were observed with decrease in fluorescence lifetime when BSA interacted with TiO2 NPs and silver NPs [32,33]. While increasing concentrations of CuO NPs in BSA, lifetime of BSA-CuO NP complex gradually increased for lifetime T1 whereas an increase and then decrease in fluorescence lifetime was observed for lifetime T2 ( fig.…”

Section: Time-resolved Fluorescence Analysissupporting

confidence: 83%

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

Abraham

Parthasarathy

2018

Int J Pharm Pharm Sci

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Objective: Since structural changes of adsorbed protein are necessary for cellular uptake of nanoparticles (NPs) it is of prime importance to know about structural changes of bovine serum albumin (BSA) when it interacts with CuO NPs-a potential new antitumor drug.Methods: CuO NPs prepared by sol-gel technique were characterized by x-ray diffraction (XRD) and tunneling electron microscope (TEM) techniques. The conformational changes induced by CuO NPs on BSA were studied by various spectroscopic techniques such as steady state and time-resolved fluorescence measurements. The changes in fluorescence emission parameters such as fluorescence intensity, fluorescence emission maximum and lifetimes of fluorescent residues in BSA were studied.Results: XRD analysis showed the average particle size as 32 nm. The TEM micrograph showed particles of different size varying from 10 to 45 nm. Fluorescence quenching was confirmed due to a decrease in fluorescence intensity of CuO NPs-BSA complex. The analysis of lifetime measurements indicated BSA contained two tryptophan (trp) residues that fluoresced in different environments. Static quenching mechanism was confirmed by time-resolved measurements when BSA interacted with CuO NPs. Conclusion:Minor structural changes of BSA protein were observed during the interaction studies.

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Section: Time-resolved Fluorescence Analysissupporting

confidence: 83%

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

Abraham

Parthasarathy

2018

Int J Pharm Pharm Sci

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“…The full with half maxima value for native BSA was 33.02 nm (curve a) and for BSA NPs the peak broadened to 52.82 nm, 65.98 nm and 66.42 nm for 25, 50 and 100 mg/mL concentration respectively (curves b-d). These data clearly indicate that there are some conformational transitions which are obtained due to NPs formation and may also be attributed due to the different conformations of BSA NPs [26,27]. It was remarkable that as the concentration of BSA increases the peak broadening also increases which may be due to the decrease in size of BSA NPs.…”

Section: Absorption Spectroscopy Of Bsa Npsmentioning

confidence: 81%

Investigating the influence of effective parameters on molecular characteristics of bovine serum albumin nanoparticles

Rohiwal

Satvekar

Tiwari

et al. 2015

Applied Surface Science

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“…In two of these studies, short-range attraction potentials were added to model the binding of statherin protein on pure hydrophobic, charged, and mixed surfaces (Skepö, 2008), and the binding of β-casein on hydrophobic and charged surfaces (Evers et al 2012). Further, MC simulations of bovine serum albumin (BSA) and HSA on silver nanoparticles using a CG model elucidated conformational changes of the protein upon adsorption, which were found to be in agreement with measured tryptophan adsorption spectra (Voicescu et al 2012). …”

Section: Coarse-grained Molecular Mechanics Modeling Of Protein-surfamentioning

confidence: 83%

Modeling and simulation of protein–surface interactions: achievements and challenges

Ozboyaci

Kokh

Corni

et al. 2016

Quart. Rev. Biophys.

197

199

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Abstract. Understanding protein-inorganic surface interactions is central to the rational design of new tools in biomaterial sciences, nanobiotechnology and nanomedicine. Although a significant amount of experimental research on protein adsorption onto solid substrates has been reported, many aspects of the recognition and interaction mechanisms of biomolecules and inorganic surfaces are still unclear. Theoretical modeling and simulations provide complementary approaches for experimental studies, and they have been applied for exploring protein-surface binding mechanisms, the determinants of binding specificity towards different surfaces, as well as the thermodynamics and kinetics of adsorption. Although the general computational approaches employed to study the dynamics of proteins and materials are similar, the models and force-fields (FFs) used for describing the physical properties and interactions of material surfaces and biological molecules differ. In particular, FF and water models designed for use in biomolecular simulations are often not directly transferable to surface simulations and vice versa. The adsorption events span a wide range of time-and length-scales that vary from nanoseconds to days, and from nanometers to micrometers, respectively, rendering the use of multi-scale approaches unavoidable. Further, changes in the atomic structure of material surfaces that can lead to surface reconstruction, and in the structure of proteins that can result in complete denaturation of the adsorbed molecules, can create many intermediate structural and energetic states that complicate sampling. In this review, we address the challenges posed to theoretical and computational methods in achieving accurate descriptions of the physical, chemical and mechanical properties of protein-surface systems. In this context, we discuss the applicability of different modeling and simulation techniques ranging from quantum mechanics through all-atom molecular mechanics to coarse-grained approaches. We examine uses of different sampling methods, as well as free energy calculations. Furthermore, we review computational studies of protein-surface interactions and discuss the successes and limitations of current approaches.

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Spectroscopic and coarse-grained simulation studies of the BSA and HSA protein adsorption on silver nanoparticles

Cited by 48 publications

References 65 publications

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

Interaction of Copper Oxide Nanoparticles With Bovine Serum Albumin by Spectroscopic Studies

Investigating the influence of effective parameters on molecular characteristics of bovine serum albumin nanoparticles

Modeling and simulation of protein–surface interactions: achievements and challenges

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