A long-acting FSH agonist through fusing human chorionic gonadotropin beta subunits of the FSHβ

Follicle stimulating hormone (FSH) is a pituitary glycoprotein hormones, ovarian follicles and seminiferous tubules of the testis development is essential. FSH is used clinically to stimulate follicular maturation, in vitro fertilization and the treatment of anovulatory women. The clinical use of the FSH is a problem of its short half-life in circulation. In order to solve this, we construct the C-terminal peptide containing the FSHβ subunit of human chorionic gonadotropin β subunit (CG beta) translated sequence fused (FSHβ) the coding sequence of the chimeric gene. To sustain human CG dimer prolonged plasma half-life of CG test this region is very important. Did not significantly affect the component of the FSH beta with the dimer of the α subunit or secretion in the presence of the C-terminal peptide sequence. The in vitro receptor binding and steroid synthesis activity dimer bearing the the FSHβ-C-terminal peptide chimera is the same as the wild-type FSH. However, both the enhanced in vivo potency and half-life in circulation dimer bearing either one or two C-terminal peptide unit. The dimer containing FSHβ-CG Beta chimera as strong clinical use of the FSH receptor agonists, the current strategy can improve a wide range of applications in different protein half-life in the body.