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.

Highlights

  • Albumins are globular proteins commonly found in blood plasma, egg white, milk, and plants [1,2,3,4]

  • E. coli along with the chaperone proteins can increase the amount of recombinant HSA (rHSA) expressed in the soluble fraction from 10% to 60% [18] and this protein appears to be monomeric and structurally similar to Human serum albumin (HSA) purified from plasma [41]

  • The inherent properties of the human serum albumin make it highly desirable for biotechnological applications. It is commonly used in cell culture applications as a replacement for traditionally used serum

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Summary

Introduction

Albumins are globular proteins commonly found in blood plasma, egg white, milk, and plants [1,2,3,4]. It regulates the oncotic pressure and pH of the blood [5] It binds and transports various bioactive molecules, including proteins, peptides, fatty acids, hormones, amino acids, drugs, nutrients, and metal ions [6,9]. These properties make albumin an excellent candidate for several clinical and biotechnological applications. The past decade has seen HSA been extensively explored as a nanoparticle for targeted drug delivery [13] For all these applications, large quantities of HSA are classically sourced from blood serum. Fetal bovine serum (FBS) was a critical factor in eukaryotic cell cultures. This review highlights the inherent structural and biochemical features that allow human serum albumin (HSA) to be exploited for cell culture applications

Recombinant HSA
Structural and Biochemical Features of HSA
Metal Ion Interactions
The Cys-34 Metal-Binding Site
Antioxidant Features of HSA
Pyridoxal and Riboflavin Interactions
Chemical Modifications of HSA
Ligand Interactions
10. Protein Interactions
11. Protective Role of Albumin against Physical Damage in Cell Culture
12. Role of Albumins in Bioprocess Development
Findings
13. Conclusions
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