IGF-DES (Des(1-3)-IGF-1) is a naturally occurring N-terminal truncated variant of insulin-like growth factor 1 (IGF-1) that exhibits enhanced receptor-binding affinity compared to native IGF-1, making it a highly studied compound in growth factor and anabolic signaling research. Composition: 67 amino acids (7.4 kDa molecular weight) — three N-terminal amino acids (Gly-Pro-Glu) removed relative to native IGF-1. Key Structural Features: - N-terminal truncation eliminates the first three amino acid residues (des(1-3)) - Altered N-terminal domain disrupts IGFBP (insulin-like growth factor binding protein) interaction - Preserved C-domain and A-domain maintain full IGF-1R binding epitopes - Enhanced receptor affinity relative to both native IGF-1 and IGF-1 LR3 IGFBP Interaction: Significantly reduced binding to IGFBP-1, -2, and -3 due to N-terminal truncation, resulting in higher free peptide fraction in biological assays. IGF-DES binds the IGF-1 receptor with approximately 2-10x g
IGF-DES: Truncated IGF-1 Analog and Receptor Binding Research Guide
Understanding IGF-DES (Des(1-3)-IGF-1), the N-terminal truncated IGF-1 variant with enhanced receptor-binding affinity and reduced IGFBP interaction for anabolic pathway research.