The Tesamorelin sequence is a stabilized version of human GHRH that features an anchored hexenoic acid moiety at the N-terminal end. This structural modification is critical because it protects the peptide from rapid enzymatic degradation by dipeptidyl peptidase-4 (DPP-4), which typically cleaves native GHRH. By resisting this degradation, Tesamorelin maintains a significantly longer biological half-life and provides sustained activation of the GHRH receptor (GHRHR) in the anterior pituitary, facilitating a robust pulsatile release of growth hormone without disrupting natural feedback loops.