Investigation on PEGylation strategy of recombinant human interleukin-1 receptor antagonist

Although PEGylation is a potential approach to prolong the half-lives and reduce the dosing frequency of therapeutic proteins, conjugation behaviors of polymer have pivotal effects on the remaining bioactivities of the derivatives. In this study, the PEGylation strategy of recombinant human interleukin-1 receptor antagonist was investigated. The random conjugation of polyethylene glycol to amino groups on the protein resulted in a severe loss of activity and only retained 9.8% of the activity. In contrast, the PEGylation at the thiol groups had moderate effects on the bioactivity of protein and 40% of activity was conserved. The results suggested that the thiol-target PEGylation was more beneficial for IL-1ra.

The PEGylated strategy of recombinant human interleukin-1 receptor antagonist was investigated, and we found that the random conjugation of polyethylene glycol to amino groups on the protein resulted in a severe loss of activity (9.8% of unmodified protein) and PEGylation at the thiol groups was desirable (40% of unmodified protein). The results suggested that the thiol-target PEGylation was more beneficial for IL-1ra.Figure optionsDownload as PowerPoint slide