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“School of Nano-Sciences”

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Paper   IPM / Nano-Sciences / 13704
School of Nano Science
  Title:   An in-depth view of human serum albumin corona on gold nanoparticle
  Author(s): 
1.  Fatemeh Ramezani
2.  Hashem Rafii-Tabar
  Status:   Published
  Journal: Mol. BioSys
  No.:  2
  Vol.:  11
  Year:  2015
  Pages:   454-462
  Publisher(s):   The Royal Society of Chemistry
  Supported by:  IPM
  Abstract:
Upon entering biological systems, such as the blood stream, nanoparticles form molecular complexes with the proteins encountered called protein coronas, which shield the surface of the exogenous nanoparticle. The most abundant blood proteins, such as albumin, initially occupy the surface of the nanoparticle. Owing to the widespread applications of gold nanoparticles in medicine, in this study, the docking of human serum albumin to gold nanoparticles was examined and the changes in protein structure were investigated by a molecular dynamic simulation and GOLP force field. The results showed that after the adsorption of albumin on the gold nanoparticle, human serum albumin was denatured and the amount of alpha-helix significantly decreased. Domain III, which has a large cavity of fatty acids binding sites, plays an important role in the adsorption on the gold nanoparticles. Lys464, Thr504, Phe505, and Leu581 are critical amino acids in HSA adsorption on the GNPs. After the adsorption of albumin on the surface of gold nanoparticles, the fluctuations in some of the domains of the protein increased. Variations in the helix properties, such as helix length, dipole, radius, average phi and psi angles, and the length of hydrogen bonds, were calculated in detail.

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