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Research Catalog

Compound monograph

Orforglipron

Orforglipron is a synthetic nonpeptide molecule characterized as a selective, high-affinity agonist at the human GLP-1 receptor.

Published: 2026-09-12Last updated: 2026-09-15Literature/identifier verification: 2026-08-23
Also known asLY3502970
Nonpeptide receptor agonists

01

Identity & nomenclature

Orforglipron is a synthetic nonpeptide molecule characterized as a selective, high-affinity agonist at the human GLP-1 receptor.

Orforglipron is a nonpeptide small molecule, not a peptide. It is documented in this library because it is characterized at the GLP-1 receptor, the same receptor as the peptide analogs semaglutide, liraglutide and exenatide, and because the cited structural work compares nonpeptide and peptide binding at that receptor. The development code LY3502970 appears in the PubChem synonym set and throughout the primary literature; both designations resolve to the same molecular record.

Declared aliases and development codes: LY3502970.

02

Molecular properties

Molecular formulaC48H48F2N10O5
Molecular mass883 Da
CAS Registry Number2212020-52-3
PubChem CID137319706
UNII7ZW40D021M

03

Structural characteristics

Orforglipron is a nonpeptide agonist of the receptor activated by endogenous GLP-1. Residue substitutions relative to GLP-1 are not applicable, rather than unknown or undetermined: this molecule is not a peptide and has no sequence to align. The related GLP-1(7-36) amide entry is a native receptor comparator only, not a structural parent. Competition binding experiments report orforglipron as a high-affinity ligand of the human GLP-1 receptor with an inhibition constant of approximately 1 nM. Signal transduction assays report low intrinsic activation of downstream effectors and negligible beta-arrestin recruitment. Structural work on the same molecule reports a high-resolution active-state receptor structure in which the nonpeptide agonist occupies a binding pocket in the upper helical bundle that is distinct from the peptide-binding mode, which is the basis for comparing the two ligand classes at a single receptor.

04

Molecular targets & mechanisms

Glucagon-like peptide-1 receptor

GLP-1R

GLP-1R is a class B G-protein-coupled receptor. The cited structural and pharmacology records characterize semaglutide and retatrutide as peptide agonists at this receptor.

05

Analytical considerations

As a nonpeptide molecule the analytical considerations differ from the peptides in this library: there is no amino acid sequence to confirm, and the two fluorine atoms in the molecular formula are relevant to mass-based identity confirmation.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

  • Competition binding assays at the human GLP-1 receptor with radiolabeled GLP-1 or orforglipron

    In competition binding assays at the human GLP-1 receptor using radiolabeled GLP-1 or orforglipron, the study reported an inhibition constant (Ki) of 1 nM for orforglipron.

    Reference [1]

  • Human GLP-1 receptor signal-transduction assays

    In human GLP-1 receptor signal-transduction assays, the study measured low intrinsic effector activation and negligible β-arrestin recruitment by orforglipron.

    Reference [1]

  • GLP-1 receptor signaling assays

    In GLP-1 receptor signaling assays, the study reported that LY3502970 was a partial agonist biased toward G protein activation over β-arrestin recruitment.

    Reference [2]

  • Active-state GLP-1 receptor structural preparation

    Using an active-state GLP-1 receptor structural preparation, the study identified a LY3502970 binding pocket involving the extracellular domain, extracellular loop 2 and transmembrane helices 1, 2, 3 and 7.

    Reference [2]

Animal studies

  • Mice expressing the human GLP-1 receptor during glucose tolerance testing

    In mice expressing the human GLP-1 receptor during glucose tolerance testing, the study observed a full biological response to orforglipron despite low predicted receptor occupancy.

    Reference [1]

06

Verified bibliography

Cited studies by type

The 2 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

  1. Reference 1

    The pharmacological basis for nonpeptide agonism of the GLP-1 receptor by orforglipron.

    Sloop KW, Cox AL, Wainscott DB, White A, Droz BA, Stutsman C, Showalter AD, Suter TM, Dunbar JD, Snider BM, O'Farrell LS, Hewitt N, Ruble JC, Padgett LR, Woerly EM, Peterson JA, Coskun T, Liu Z, Coutant DE, Ai M, Emmerson PJ, Sangwung P, Willard FS

    Science translational medicine · 2024-12-18 · Journal Article

    current
    PMID 39693407DOI 10.1126/scitranslmed.adp5765OrforglipronGLP-1R

  2. Reference 2

    Structural basis for GLP-1 receptor activation by LY3502970, an orally active nonpeptide agonist.

    Kawai T, Sun B, Yoshino H, Feng D, Suzuki Y, Fukazawa M, Nagao S, Wainscott DB, Showalter AD, Droz BA, Kobilka TS, Coghlan MP, Willard FS, Kawabe Y, Kobilka BK, Sloop KW

    Proceedings of the National Academy of Sciences of the United States of America · 2020-11-11 · Journal Article

    current
    PMID 33177239PMC7703558DOI 10.1073/pnas.2014879117LiraglutideOrforglipronGLP-1R

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

ReferenceStudy models
Sloop KW et al. 2024Study models reported: in vitro; animal (mouse, rat) · from the abstract
Kawai T et al. 2020Study models reported: in vitro; animal (mouse, rat, cynomolgus monkey) · from the full text

Record history

Published 2026-09-12.

  • : Sequence and structure

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. Orforglipron. Published 2026-09-12; updated 2026-09-15. https://purelypeptides.org/research/compounds/orforglipron/

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

Read the full methodology →