Researchers made a combined protein that joins interferon‑alpha2 and thymosin‑alpha1, showed they could produce it in bacteria at high levels, and found it kills cancer cells better than interferon alone, but the work is all lab‑based and doesn’t give any dosing or safety info for people to use.

The use of interferon &#x3b1;-2 in combination with thymosin &#x3b1;-1 shows higher anti-cancer effect in comparison when both are used individually because of their synergistic effects. In this study we produced an important human interferon &#x3b1;-2-thymosin &#x3b1;-1 (IFN&#x3b1;2-T&#x3b1;1) fusion protein with probable pharmaceutical properties coupled to its high-level expression, characterization, and study of its biological activity. The IFN&#x3b1;2-T&#x3b1;1 fusion gene was constructed by over-lap extension PCR and expressed in <i>Escherichia coli</i> expression system. The expression of IFN&#x3b1;2-T&#x3b1;1 fusion protein was optimized to higher level and its maximum expression was obtained in modified terrific broth medium when lactose was used as inducer. The fusion protein was refolded into its native biologically active form with maximum yield of 83.14% followed by purification with &#x223c;98% purity and 69% final yield. A band of purified IFN&#x3b1;2-T&#x3b1;1 fusion protein equal to &#x223c;23&#x2009;kDa was observed on 12 % SDS-PAGE gel. The integrity of IFN&#x3b1;2-T&#x3b1;1 fusion protein was confirmed by western blot analysis and secondary structure was assessed by CD spectroscopy. When IFN&#x3b1;2-T&#x3b1;1 fusion protein was subjected to its biological activity analysis it was observed that it exhibits both IFN&#x3b1;2 &amp; T&#x3b1;1 activities as well as significantly higher anticancer activity as compared to IFN&#x3b1;-2 alone.