Researchers made a slightly altered version of thymosin‑alpha‑1 by swapping the last amino‑acid for its D‑form and adding an acetyl group at the start. This new peptide still helped weak T‑cells from kidney‑failure patients respond better, and it stayed intact much longer in human serum than the regular peptide. The changes make the molecule more resistant to breakdown, which could mean a longer‑lasting immune boost.

A fragment analog, [D-Arg30]prothymosin alpha fragment 1-30, containing D-arginine in place of arginine residue at position 30 was synthesized by the liquid phase procedure and studied for immunological effect on the impaired blastogenic response of T-lymphocytes isolated from uremic patients after treatment of human serum. Deacetyl-thymosin alpha 1, a synthetic octaeicosapeptide corresponding to deacetyl-prothymosin alpha fragment 1-28, has restoration ability for the impaired blastogenic response of T-lymphocytes of uremic patients but is susceptible to proteolytic digestion. On the other hand, the fragment analog, [D-Arg30]prothymosin alpha fragment 1-30 retained activity and was shown to exhibit a high degree of stability when incubated in human serum. These results indicate that N-terminal acetylation and the introduction of D-residue into the C-terminal residue of prothymosin alpha fragment 1-30 increase resistance to proteolytic degradation by exopeptidases.