scholarly journals Biogenic Ferrihydrite Nanoparticles Produced by Klebsiella oxytoca: Characterization, Physicochemical Properties and Bovine Serum Albumin Interactions

Nanomaterials ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 249
Nicoleta Cazacu ◽  
Claudia G. Chilom ◽  
Sorina Iftimie ◽  
Maria Bălășoiu ◽  
Valentina P. Ladygina ◽  

The synthesis of nanoparticles inside microorganisms is an economical alternative to chemical and physical methods of nanoparticle synthesis. In this study, ferrihydrite nanoparticles synthesized by Klebsiella oxytoca bacterium in special conditions were characterized by scanning electron microscopy (SEM), energy-dispersive X-ray analysis (EDS), small-angle X-ray (SAXS), UV-Vis spectroscopy, fluorescence, fluorescence resonance energy transfer (FRET), and molecular docking. The morphology and the structure of the particles were characterized by means of SEM and SAXS. The elemental content was determined by means of the EDS method. The absorption properties of the ferrihydrite nanoparticles were investigated by UV-Vis spectroscopy. The binding mechanism of the biogenic ferrihydrite nanoparticles to Bovine Serum Albumin (BSA) protein, studied by fluorescence, showed a static and weak process, combined with FRET. Protein denaturation by temperature and urea in the presence of the ferrihydrite nanoparticles demonstrated their influence on the unfolding process. The AutoDock Vina and UCSF Chimera programs were used to predict the optimal binding site of the ferrihydrite to BSA and to find the location of the hydrophobic cavities in the sub-domain IIA of the BSA structure.

2020 ◽  
Nicoleta Sandu ◽  
Claudia G. Chilom ◽  
Melinda David ◽  
Monica Florescu

ABSTRACTBovine serum albumin (BSA) acts as a carrier for many endogenous and exogenous compounds, such as thyroid hormones or corresponding drugs. Binding of the hydrophilic compound levothyroxine (LT4) to BSA can significantly alter the pharmacological properties of the compound. Therefore, studying its interaction with BSA could be a difficult issue. In this work, the binding mechanism and affinity of the interaction between LT4 and BSA were investigated, both in solution using UV-Vis, Fourier-transform infrared spectroscopy (FT-IR), fluorescence and fluorescence resonance energy transfer (FRET), as well as by Surface Plasmon Resonance (SPR) with BSA confined to a gold-coated chips, as far as we know for the first time used to study the interactions between LT4 and proteins. Quenching of BSA fluorescence by LT4 combined with UV-Vis spectroscopy shows a ground-state complex formation that may be accompanied by a nonradiative energy transfer process. FT-IR revealed the changes induced by LT4 in the secondary structure of BSA molecules, due to the partial unfolding of BSA native structure upon LT4 binding. Scatchard approach allowed the determination of the binding constant and the thermodynamic parameters, which correspond to an enthalpic process, driven mainly by hydrogen bonds and van der Waals forces. Using SPR, the adsorbed amount of biomolecules was calculated and the binding affinity of LT4 with confined-BSA was characterized using the Hill-Langmuir equation, indicating that the BSA immobilization plays an important role in LT4 binding. As preliminary results, both fluorescence quenching and SPR can be used as a stepping stone for the development of a spectroscopic biosensor for LT4 detection, with a limit of detection as low as 0.23 × 10−6 M.

Langmuir ◽  
2012 ◽  
Vol 28 (47) ◽  
pp. 16306-16317 ◽  
Yolanda S. Hedberg ◽  
Manuela S. Killian ◽  
Eva Blomberg ◽  
Sannakaisa Virtanen ◽  
Patrik Schmuki ◽  

Materials ◽  
2021 ◽  
Vol 14 (2) ◽  
pp. 298
Shufang Liu ◽  
Shu’e Wang ◽  
Zhanzuo Liu

The morphology of nanomaterials may affect their interaction with biomacromolecules such as proteins. Previous work has studied the size-dependent binding of pristine nC60 to bovine/human serum albumin using the fluorometric method and found that the fluorescence inner filter effect might affect this interaction. However, if it is necessary to accurately calculate and obtain binding information, the fluorescence inner filter effect should not be ignored. This work aimed to further investigate the effect of the fluorescence inner filter on the interaction between pristine nC60 with different particle sizes (140–160, 120–140, 90–110, 50–70, and 30–50 nm) and bovine serum albumin for a more accurate comprehension of the binding of pristine nC60 to bovine serum albumin. The nC60 nanoparticles with different size distributions used in the experiments were obtained by the solvent displacement and centrifugation method. UV-Vis spectroscopy and fluorescence spectroscopy were used to study the binding of nC60 with different size distributions to bovine serum albumin (BSA) before and after eliminating the fluorescence inner filter effect. The results showed that the fluorescence inner filter effect had an influence on the interaction between nC60 and proteins to some extent, and still did not change the rule of the size-dependent binding of nC60 nanoparticles to BSA. Further studies on the binding parameters (binding constants and the number of binding sites) between them were performed, and the effect of the binding on BSA structures and conformation were also speculated.

RSC Advances ◽  
2017 ◽  
Vol 7 (42) ◽  
pp. 26250-26255 ◽  
Arun Singh Patel ◽  
Praveen Mishra ◽  
Pawan K. Kanaujia ◽  
Syed Shariq Husain ◽  
G. Vijaya Prakash ◽  

The resonance energy transfer (RET) from tryptophan present in bovine serum albumin (BSA) to two dimensional (2D) nanomaterials has been reported.

2013 ◽  
Vol 538 ◽  
pp. 301-304
Yi Ping Zhong ◽  
Rui Bin Hong ◽  
Bin Bin Yin ◽  
Ping Liu ◽  
Wen Ji Deng

The water-soluble conjugated polyelectrolyte, poly[3-(1′-propyloxy-3′-sodium sulfonate) thiophene] (PTH-n3-SO3Na), was prepared. The interaction between the PTH-n3-SO3Na and bovine serum albumin (BSA) was investigated using UV-vis spectroscopy. It was found that the PTH-n3-SO3Na could be used as biosensor to detect BSA.

Polymers ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 2603
Andra Mihaela Onaș ◽  
Iuliana Elena Bîru ◽  
Sorina Alexandra Gârea ◽  
Horia Iovu

This study investigates the formation of a graphene oxide-polyamidoamine dendrimer complex (GO-PAMAM) and its association and interaction with bovine serum albumin (BSA). Fourier-transform infrared spectrometry and X-ray photoelectron spectrometry indicated the formation of covalent linkage between the GO surface and PAMAM with 7.22% nitrogen content in the GO-PAMAM sample, and various interactions between BSA and GO-PAMAM, including π-π* interactions at 291.5 eV for the binding energy value. Thermogravimetric analysis highlighted the increasing thermal stability throughout the modification process, from 151 to 192 °C for the 10% weight loss temperature. Raman spectrometry and X-ray diffraction analysis were used in order to examine the complexes’ assembly, showing a prominent (0 0 2) lattice in GO-PAMAM. Dynamic light scattering tests proved the formation of stable graphenic and graphenic-protein aggregates. The secondary structure rearrangement of BSA after interaction with GO-PAMAM was investigated using circular dichroism spectroscopy. We have observed a shift from 10.9% β-sheet composition in native BSA to 64.9% β-sheet composition after the interaction with GO-PAMAM. This interaction promoted the rearrangement of the protein backbone, leading to strongly twisted β-sheet secondary structure architecture.

Materials ◽  
2020 ◽  
Vol 13 (19) ◽  
pp. 4269 ◽  
Ewa Paradowska ◽  
Katarzyna Arkusz ◽  
Dorota G. Pijanowska

The increasing interest of attachment of gold nanoparticles (AuNPs) on titanium dioxide nanotubes (TNTs) has been devoted to obtaining tremendous properties suitable for biosensor applications. Achieving precise control of the attachment and shape of AuNPs by methods described in the literature are far from satisfactory. This work shows the comparison of physical adsorption (PA), cyclic voltammetry (CV) and chronoamperometry (CA) methods and the parameters of these methods on TNTs properties. The structural, chemical, phase and electrochemical characterizations of TNTs, Au/TNTs, AuNPs/TNTs are carried out using scanning electron microscopy (SEM), electrochemical impedance spectroscopy, X-ray diffraction, X-ray photoelectron spectroscopy. The use of PA methods does not allow the deposition of AuNPs on TNTs. CV allows easily obtaining spherical nanoparticles, for which the diameter increases from 20.3 ± 2.9 nm to 182.3 ± 51.7 nm as a concentration of tetrachloroauric acid solution increase from 0.1 mM to 10 mM. Increasing the AuNPs deposition time in the CA method increases the amount of gold, but the AuNPs diameter does not change (35.0 ± 5 nm). Importantly, the CA method also causes the dissolution of the nanotubes layer from 1000 ± 10.0 nm to 823 ± 15.3 nm. Modification of titanium dioxide nanotubes with gold nanoparticles improved the electron transfer and increased the corrosion resistance, as well as promoted the protein adsorption. Importantly, after the deposition of bovine serum albumin, an almost 5.5-fold (324%) increase in real impedance, compared to TNTs (59%) was observed. We found that the Au nanoparticles—especially those with smaller diameter—promoted the stability of bovine serum albumin binding to the TNTs platform. It confirms that the modification of TNTs with gold nanoparticles allows the development of the best platform for biosensing applications.

2005 ◽  
Vol 5 (4) ◽  
pp. 331-336 ◽  
Sabrina M. Pancera ◽  
Rosangela Itri ◽  
Denise F. S. Petri

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