Abaloparatide is a parathyroid hormone-related protein (PTHrP) analog drug in clinical development for treating osteoporosis. Like the related drug teriparatide, and unlike bisphosphonates, it is an anabolic (i.e., bone growing) agent.
CAT No: 10-101-172
CAS No:247062-33-5
Synonyms/Alias:Abaloparatide;247062-33-5;Abaloparatide acetate;XJA06233;H-DL-Ala-DL-Val-DL-Ser-DL-Glu-DL-His-DL-Gln-DL-Leu-DL-Leu-DL-His-DL-Asp-DL-Lys-Gly-DL-Lys-DL-Ser-DL-xiIle-DL-Gln-DL-Asp-DL-Leu-DL-Arg-DL-Arg-DL-Arg-DL-Glu-DL-Leu-DL-Leu-DL-Glu-DL-Lys-DL-Leu-DL-Leu-Aib-DL-Lys-DL-Leu-DL-His-DL-xiThr-DL-Ala-NH2;
Abaloparatide is a synthetic peptide analog of human parathyroid hormone-related protein (PTHrP), designed to selectively activate the parathyroid hormone 1 receptor (PTH1R). As a 34-amino acid peptide, it mimics the functional domain of PTHrP, enabling precise modulation of PTH1R-mediated signaling pathways. Its unique structural modifications confer distinct receptor binding kinetics and downstream signaling profiles, making it a valuable tool for dissecting the physiological and biochemical roles of PTH1R. Abaloparatide's high specificity and receptor selectivity have established it as a prominent research reagent in bone metabolism, peptide-receptor interaction studies, and related fields of endocrine regulation.
Receptor Pharmacology: In the context of receptor pharmacology, abaloparatide is widely employed to investigate the activation mechanisms and signal transduction events of the parathyroid hormone 1 receptor. Its capacity to induce transient versus sustained cAMP responses enables researchers to differentiate between ligand-biased signaling pathways. By utilizing this peptide, scientists can dissect the structural determinants of PTH1R activation and elucidate the downstream molecular events that govern cellular responses in bone and mineral metabolism.
Peptide-Structure Activity Relationship Studies: Abaloparatide serves as an essential reference molecule in structure-activity relationship (SAR) analyses of peptide ligands targeting PTH1R and related G protein-coupled receptors. Its engineered amino acid substitutions and altered receptor affinity profiles provide a benchmark for comparing the functional consequences of sequence modifications. Researchers leverage this peptide to design and evaluate novel analogs, furthering the understanding of how specific residues influence receptor binding, activation, and selectivity.
Bone Metabolism Research: As a potent PTH1R agonist, abaloparatide is a critical tool in studies examining the cellular and molecular mechanisms underlying bone formation and resorption. Researchers use it to model anabolic signaling cascades in osteoblasts and to probe the regulatory networks that control skeletal remodeling. Its application in in vitro and ex vivo systems allows for the detailed characterization of gene expression changes, cytokine release, and matrix synthesis in response to PTH1R activation.
Peptide Stability and Delivery Investigations: The unique structural features of abaloparatide, such as its enhanced resistance to proteolytic degradation, make it particularly valuable in studies focused on peptide stability and delivery. Scientists utilize the peptide to assess the impact of sequence modifications on metabolic stability in biological matrices, as well as to develop and optimize delivery systems for peptide-based agents. These investigations inform strategies for improving peptide bioavailability and functional longevity in experimental settings.
Endocrine Signaling Pathway Analysis: Abaloparatide is frequently used to probe the broader landscape of endocrine signaling pathways governed by PTH1R. Its well-characterized receptor interactions facilitate the mapping of cross-talk between PTH1R-mediated cascades and other hormonal or metabolic pathways. Through controlled application in cellular and tissue models, researchers can delineate the physiological relevance of PTH1R activation in diverse biological systems, advancing the overall understanding of endocrine regulation and homeostasis.
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