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The molecule retains the complete 70-amino-acid native IGF-1 sequence with two structural modifications a 13-amino-acid N-terminal extension (the Long designation) and an arginine-for-glutamic-acid substitution at position 3 (the R3 designation) which together reduce binding affinity to circulating IGF binding proteins (IGFBPs) by approximately 600-fold while preserving full agonist activity at the IGF-1 receptor

Schroeder U, Himpe B, Pries R, Vonthein R, Nitsch S, Wollenberg B