Effect of genetic variation on the thermal stability of human serum albumin

Author(s):  
Ulrich Kragh-Hansen ◽  
Shiori Saito ◽  
Koji Nishi ◽  
Makoto Anraku ◽  
Masaki Otagiri
2016 ◽  
Vol 11 (4) ◽  
pp. 04B310 ◽  
Author(s):  
Robin Capomaccio ◽  
Inês Osório ◽  
Isaac Ojea-Jiménez ◽  
Giacomo Ceccone ◽  
Pascal Colpo ◽  
...  

2020 ◽  
Vol 142 (5) ◽  
pp. 1911-1917
Author(s):  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Svetla Todinova ◽  
Ivan Angelov ◽  
Paula Ossowicz ◽  
...  

2020 ◽  
Vol 21 (24) ◽  
pp. 9734
Author(s):  
Claudia G. Chilom ◽  
Adriana Bălan ◽  
Nicoleta Sandu ◽  
Maria Bălăşoiu ◽  
Sergey Stolyar ◽  
...  

In the last few years, a great amount of attention has been given to nanoparticles research due to their physicochemical properties that allow their use in analytical instruments or in promising imaging applications on biological systems. The use of ferrihydrite nanoparticles (Fh-NPs) in practical applications implies a particular control of their magnetic properties, stability, biocompatibility, interaction with the surface of the target, and low toxicity. In this study, the formation and organization of human serum albumin (HSA) molecules around the simple Fh-NPs and Fh-NPs doped with Co and Cu were examined by Scanning Electron Microscopy (SEM) and Atomic Force Microscopy (AFM) in terms of morphology and particle size. The topology of all Fh-NPs shows an organized area of HSA around each type of Fh-NP. Molecular docking studies were used in order to determine the probable location of the ferrihydrite in the HSA structure. The thermal stability of these nanohybrids was further investigated by fluorimetry, using 214-Trp residue from HSA as a spectral sensor. The denaturation temperature (Tm) was determined, and stabilization of the HSA structure in the presence of Fh-NPs was discussed. This study could be a starting point for the development of different applications targeting the structure and stability of Fh-NPs complexes with proteins.


RSC Advances ◽  
2015 ◽  
Vol 5 (24) ◽  
pp. 18218-18232 ◽  
Author(s):  
Mohd Ishtikhar ◽  
Gulam Rabbani ◽  
Shawez Khan ◽  
Rizwan Hasan Khan

Thymoquinone more strongly interacts with the ‘N’ isoform in comparison to the ‘B’ isoform of HSA and also increases its thermal stability but the antioxidant activity is significantly higher at the ‘B’ isoform of HSA.


PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e84552 ◽  
Author(s):  
Giuseppe Sancataldo ◽  
Valeria Vetri ◽  
Vito Foderà ◽  
Gianluca Di Cara ◽  
Valeria Militello ◽  
...  

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