Des(1-3)IGF-1 is an endogenous naturally existing protein. Meanwhile, it acts as a truncated structural analogue of insulin-like growth factor 1, commonly known as IGF-1. There is an obvious distinction in its amino acid sequence when compared with native full-length IGF-1. From a structural perspective, Des(1-3)IGF-1 removes the first three amino acid residues positioned at the N-terminus of standard IGF-1 molecule. As a result of this truncation modification, Des(1-3)IGF-1 is made up of 67 amino acids in total, whereas the complete full-length IGF-1 comprises 70 amino acids in its peptide chain.
Thanks to this distinctive structural variation at the N-terminal region, Des(1-3)IGF-1 shows markedly weakened binding capacity with insulin-like growth factor-binding proteins, generally abbreviated as IGFBPs. Less combination with IGFBPs allows more molecules to remain available and functional. Benefiting from this prominent structural advantage, this peptide delivers greatly enhanced biological activity. Under in vivo experimental environments, its functional potency reaches approximately 10 times higher compared with conventional standard IGF-1, showing outstanding performance advantages for relevant research applications.
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