Proteins modified by ELP can effectively improve the circulating half-life

Compared with small molecule drugs, protein drugs have the advantages of high specificity, high activity, low toxicity and so on. There many recombinant human proteins drugs in the market. However, the circulating half-life of most protein drugs in vivo is short with low bioavailability and great side effects. Using modified protein drugs (PEG-based) or employing source albumin (HSA) fusion protein drug (HSA fusion) with polyethylene glycol (PEG) is a common way to improve the above problems, but there are obvious shortcomings, such as: biological activity of the outcomes is significantly reduced; complex process of production; low yield; high cost. Therefore, how to improve the efficiency of circulating half-life of proteins in vivo and the treatment is a very challenging biomedical problem.

Gao Weiping Study Group at Tsinghua University takes the lead to come up with a new, universal, simple and efficient method of elastin-like polypeptide fusion (ELP fusion) to design for precise protein - polymer conjugate. By fusing elastin-like polypeptide with interferon -α and using Escherichia coli to produce IFN-ELP fusion protein can get high yield and low cost, and it also keeps the biological activity of IFN-α. Model tests in mice found that proteins modified by ELP can effectively improve the circulating half-life in vivo and residence condition of tumor, eventually significantly improving the outcomes of patients and improving the survival rate of mice.

This method is expected to become a new strategy for protein modification drugs, improving drug stability, improving drug half-life and enhancing the therapeutic efficacy.

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