Effects of protein denaturation on the rotational reorientation kinetics of dansylated bovine serum albumin

1993 ◽  
Vol 97 (41) ◽  
pp. 10872-10878 ◽  
Author(s):  
Run Wang ◽  
Frank V. Bright
2004 ◽  
Vol 107 (2) ◽  
pp. 175-187 ◽  
Author(s):  
Valeria Militello ◽  
Carlo Casarino ◽  
Antonio Emanuele ◽  
Antonella Giostra ◽  
Filippo Pullara ◽  
...  

RSC Advances ◽  
2017 ◽  
Vol 7 (15) ◽  
pp. 9393-9401 ◽  
Author(s):  
Gongke Wang ◽  
Yanfang Lu ◽  
Huimin Hou ◽  
Yufang Liu

The binding of BSA to AgNPs will open a door to fully understand the essence of the interactions between nanoparticles and proteins.


Molecules ◽  
2014 ◽  
Vol 19 (4) ◽  
pp. 4880-4896 ◽  
Author(s):  
Izabela Sadowska-Bartosz ◽  
Sabina Galiniak ◽  
Grzegorz Bartosz

Nanomaterials ◽  
2022 ◽  
Vol 12 (2) ◽  
pp. 249
Author(s):  
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.


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