The study found that the LR3 version of IGF‑1, which is altered to avoid binding proteins, actually worked worse than normal IGF‑1 in turkey muscle cells, and that changes meant to dodge binding proteins can also lower the peptide’s ability to stick to its main receptor.

The effects of several human and chicken insulin-like growth factor (IGF) analogs on turkey satellite cell and embryonic myoblast proliferation were examined in serum-free medium. Similar rates of proliferation were observed when human or chicken IGF-I or IGF-II (13.1 nM) was administered to satellite cells. The biopotency of two analogs, which were modified to prevent interaction with IGF-binding proteins, was also examined. Human Des(1-6)IGF-II was equipotent to native human and chicken IGF-II. However, the chicken LR3 IGF-I analog was significantly less active toward satellite cells and embryonic myoblasts compared with chicken IGF-I. Human [Leu27] IGF-II, an analog designed to have reduced affinity to the IGF Type I receptor but unaltered binding to IGF-binding proteins, had a diminished effect on cell proliferation. Examination of IGF receptor binding characteristics revealed that chicken LR3 IGF-I had reduced ability to compete with [125I]hIGF-I for binding to satellite cells or embryonic myoblasts compared with chicken IGF-I. The observed biological responses to IGF suggest that IGF-binding proteins have little effect on Type I IGF receptor action in these cell types in serum-free medium. The results also suggest that alterations of the IGF molecule to prevent interaction with binding proteins may also alter receptor binding affinity.