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Review
. 2021 Aug 5;22(16):8411.
doi: 10.3390/ijms22168411.

Structural and Biochemical Features of Human Serum Albumin Essential for Eukaryotic Cell Culture

Vibhor Mishra  1 , Richard J Heath  1
Affiliations
Review

Structural and Biochemical Features of Human Serum Albumin Essential for Eukaryotic Cell Culture

Vibhor Mishra et al. Int J Mol Sci. .

Abstract

Serum albumin physically interacts with fatty acids, small molecules, metal ions, and several other proteins. Binding with a plethora of bioactive substances makes it a critical transport molecule. Albumin also scavenges the reactive oxygen species that are harmful to cell survival. These properties make albumin an excellent choice to promote cell growth and maintain a variety of eukaryotic cells under in vitro culture environment. Furthermore, purified recombinant human serum albumin is mostly free from impurities and modifications, providing a perfect choice as an additive in cell and tissue culture media while avoiding any regulatory constraints. This review discusses key features of human serum albumin implicated in cell growth and survival under in vitro conditions.

Keywords: cell culture; human serum albumin; ligand binding.

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Domain organization of human serum albumin. Domain I (red), domain II (blue), and domain III (green). The 3-D model was generated by PyMOL using 1AO6 PDB file.
Figure 2
Figure 2
A comparison of surface charge distribution between HSA (A,B) and BSA (C,D). The two views for each protein structure are flipped 180° along the vertical axis. The images were generated by PyMOL using 1AO6 and 4F5S PDB files.
Figure 3
Figure 3
3-D model of HSA showing the seven fatty acid (FA) binding sites. Myristate occupying the seven sites is rendered in red spheres. The 3-D model was generated by PyMOL using 1HK4 PDB file.
See this image and copyright information in PMC

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