The pharmacokinetics of a hybrid peptide consisting of the N-terminal biologically active region of human parathyroid hormone (PTH) linked to a collagen binding domain (CBD) were evaluated in female Sprague-Dawley rats. The peptide, PTH-CBD, consists of the first 33 amino acids of PTH linked as an extension of the amino acid chain to the CBD peptide derived from ColH collagenase of Clostridium histolyticum. Serum concentrations arising from single dose administration by the subcutaneous and intravenous routes were compared to those measured following route specific mole equivalent doses of PTH(1-34). Population-based modeling demonstrated similar systemic absorption kinetics and bioavailability for both peptides. Exposure to PTH-CBD was 6-fold higher due to a systemic clearance of approximately 20% relative to PTH(1-34); however, these kinetics were consistent with >95% of a dose being eliminated from serum within 24 hours. Results obtained support continued investigation of PTH-CBD as a bone targeted anabolic agent for the treatment of post-menopausal osteoporosis.