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HSA Fusion Protein Production Service

HSA Fusion Protein Production Service

Human serum albumin (HSA) is the most abundant soluble protein in human plasma, which is composed of 585 amino acids with a molecular weight of about 66.5 kDa. The half-life of HSA in human body is about 19 days. Additionally, it has the advantages of safety, non-toxicity, good biocompatibility and low immunogenicity. HSA is an ideal drug carrier, so it can be used for the long-term transformation of protein or polypeptide drugs by chemical modification or gene fusion. In 2014, FDA approved the first HSA fusion protein drug, albighztide (tanzeum), which is a DPP-4-resistant GLP-1-HSA fusion protein. HSA fusion protein as therapeutics plays an important role in drug development, especially in cancer therapy.

Overview of various HSA-based cancer therapeutics Figure 1. Overview of various HSA-based cancer therapeutics (Tao H Y, et al. 2021).

There are several benefits that HSA fused to polypeptides or other therapeutics:

  • Increase the bioavailability and prolongate the serum half-life of target protein;
  • Monomer fusion can be realized;
  • Based on the fusion at N-terminal or C-terminal, the active region of target protein could be unaffected;
  • HSA also binds FcRn, resulting in its extended half-life;
  • HSA could be expressed in yeast or E. coli to reduce the cost;
  • HSA tends to accumulate in tumors and in inflamed tissues, which helps to target proteins or peptides to those sites.

Based on our state-of-the art facilities, experiences, Profacgen can provide our customer of the HSA fusion service involved in hormones, growth factors, cytokines and peptides etc. Besides, except for gene fusion expression, we can also provide coupling services of HSA with therapeutics through covalent chemical bond or noncovalent bond.

Schematic representation of  Uox-HSA conjugate Figure 2. Schematic representation of Uox-HSA conjugate (Powell J S. et al. 2015).

Recombinant  factor IX-albumin fusion protein with a cleavable linker Figure 3. Recombinant factor IX-albumin fusion protein with a cleavable linker (Lim S I, et al, 2015)

With our in-house platform, Profacgen can develop HSA fusion modification methods according to the characteristics of protein or peptide drugs.

If you are interested in our services, please feel free to contact us . We are looking forward to cooperating with you.

References

  1. Tao H Y, Wang R Q, Sheng W J, et al. The development of human serum albumin-based drugs and relevant fusion proteins for cancer therapy[J]. International Journal of Biological Macromolecules, 2021, 187: 24-34.
  2. William R. Strohl, Fusion Proteins for Half-Life Extension of Biologics as a Strategy to Make Biobetters. BioDrugs. 2015; 29(4): 215–239.
  3. Powell J S. Longer-acting clotting factor concentrates for hemophilia[J]. Journal of Thrombosis and Haemostasis, 2015, 13: S167-S175.
  4. Lim S I, Hahn Y S, Kwon I. Site-specific albumination of a therapeutic protein with multi-subunit to prolong activity in vivo[J]. Journal of Controlled Release, 2015, 207: 93-100.
  5. Schulte S. Half-life extension through albumin fusion technologies[J]. Thrombosis research, 2009, 124: S6-S8.
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