Exploiting Soft and Hard X-Ray Absorption Spectroscopy to Characterize Metallodrug/Protein Interactions: the Binding of [trans-RuCl4(Im)(dimethylsulfoxide)][ImH] (Im = imidazole) to Bovine Serum Albumin

2008 ◽  
Vol 47 (19) ◽  
pp. 8629-8634 ◽  
Author(s):  
Isabella Ascone ◽  
Luigi Messori ◽  
Angela Casini ◽  
Chiara Gabbiani ◽  
Antonella Balerna ◽  
...  
2010 ◽  
Vol 98 (3) ◽  
pp. 630a ◽  
Author(s):  
Leandro R.S. Barbosa ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Sigrid Bernstorff ◽  
...  

2010 ◽  
Vol 98 (1) ◽  
pp. 147-157 ◽  
Author(s):  
Leandro R.S. Barbosa ◽  
Maria Grazia Ortore ◽  
Francesco Spinozzi ◽  
Paolo Mariani ◽  
Sigrid Bernstorff ◽  
...  

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

Polymers ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 2603
Author(s):  
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 ◽  
Author(s):  
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.


RSC Advances ◽  
2016 ◽  
Vol 6 (24) ◽  
pp. 19700-19706 ◽  
Author(s):  
Gongke Wang ◽  
Huimin Hou ◽  
Ye Chen ◽  
Changling Yan ◽  
Guangyue Bai ◽  
...  

The interactions between decyl-β-d-glucopyranoside (DG) and bovine serum albumin (BSA), in aqueous media, were investigated through the use of surface tension, steady-state fluorescence, and UV-vis absorption spectroscopy measurements.


2017 ◽  
Vol 19 (26) ◽  
pp. 17143-17155 ◽  
Author(s):  
Dmitry Molodenskiy ◽  
Evgeny Shirshin ◽  
Tatiana Tikhonova ◽  
Andrey Gruzinov ◽  
Georgy Peters ◽  
...  

Temperature-induced oligomerization of albumin before and after protein melting was studied using SAXS and interpreted in terms of interaction potential.


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