We studied the immunogenic properties of albeferon, the biologically active
de novo protein designed on the basis of albebetin (de novo protein with p
reassigned structure) and the octapeptide fragment of human interferon alph
a(2) (Dolgikh et al., Protein Engng., 1996, vol. 9, pp. 195-201). Rabbit an
tibodies were produced against a fusion (about 50 kDa) of albeferon with th
e maltose-binding protein. The antibodies did not interact with albeferon,
whereas they strongly interacted both with maltose-binding protein and the
fusion protein. This fact testifies that albeferon, as well as albebetin pl
aying the part of a scaffold for the active interferon fragment, has low im
munogenicity. The results show that de novo proteins with preassigned struc
ture can be constructed according to simple structural principles, and that
such proteins can serve as convenient carriers of biological activities in
the cases when low immunogenicity of active constructs is prerequisite.