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Study · Other design · 2026

5 results

Structural and mechanistic insights into dual activation of cagrilintide in amylin and calcitonin receptors.

Gu YM, Yuan QN, Li X, He Q, Xu HE, Zhao LH

Acta pharmacologica Sinica22 Aug 2025

PMID40847076 (opens in a new tab)DOI10.1038/s41401-025-01635-2 (opens in a new tab)PepBankPUB-40847076
Publisher pagePubMedAsk about this study
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Summary

The text of this summary is not shown here, because the article license does not allow reuse. Read it at the source (opens in a new tab)

Text rights: Publisher copyright. Results still quote short attributed sentences.

Results from this study5

1 result from studies that gave the peptide. No result from this study comes from people.

  1. 01LabOther designActivity measurement

    Structural and functional analyses showed that cagrilintide non-selectively activates Gs signaling through CTR and AMY1R.

    In plain wordsIn lab tests, cagrilintide switched on signaling through both the calcitonin receptor and the amylin receptor.

    Peptide
    Cagrilintide
    Outcome
    IncreaseGs signaling activation through CTR and AMY1R
    Study

    n: not reported in source

    Outcome group
    Receptor activity and mechanism · Pharmacology
    Studied dose
    Dose not stated

    Source sentences

    Summary
    Both structural and functional analyses revealed Cagri's non-selective activation of Gs signaling pathways through CTR and AMY1R.
    1 context sentence
    Summary · context
    This study elucidates the non-selective activation mechanism by determining cryo-EM structures of Cagri bound to AMY1R-Gs and CTR-Gs complexes.

Studies that did not test the peptide alone4

In this study, Cagrilintide was a lab tool or a carrier, part of a mix, or the subject of a lab method. These results are not evidence about taking Cagrilintide.

  1. 02LabNot a test of Cagrilintide aloneIn vitro (cell-free)Mechanism

    Cryo-EM structures show cagrilintide adopts similar bypass binding modes in the AMY1R and CTR receptors.

    In plain wordsIn lab tests, cagrilintide binds the amylin and calcitonin receptors in a similar way.

    Peptide
    Cagrilintide
    Outcome
    Not applicableBinding mode in AMY1R and CTR
    Study

    n: not reported in source

    Cagrilintide bound to AMY1R-Gs and CTR-Gs complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    Cagri adopts similar "bypass" binding modes in both receptors
    1 context sentence
    Summary · context
    This study elucidates the non-selective activation mechanism by determining cryo-EM structures of Cagri bound to AMY1R-Gs and CTR-Gs complexes.

    In this study, Cagrilintide was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Cagrilintide.

  2. 03LabNot a test of Cagrilintide aloneIn vitro (cell-free)Mechanism

    In the cryo-EM structures, residue F23 of cagrilintide anchors the peptide at the receptor transmembrane bundle level and the micelle.

    In plain wordsIn lab tests, one building block of cagrilintide, F23, holds the peptide in place at the receptor.

    Peptide
    Cagrilintide
    Outcome
    Not applicableF23 anchoring of cagrilintide
    Study

    n: not reported in source

    Cagrilintide bound to AMY1R-Gs and CTR-Gs complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    the F23Cagri residue anchoring the peptide at the receptor transmembrane (TM) bundle level and the micelle
    1 context sentence
    Summary · context
    This study elucidates the non-selective activation mechanism by determining cryo-EM structures of Cagri bound to AMY1R-Gs and CTR-Gs complexes.

    In this study, Cagrilintide was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Cagrilintide.

  3. 04LabNot a test of Cagrilintide aloneIn vitro (cell-free)Mechanism

    In the cryo-EM structures, an E14-R17 intramolecular salt bridge enhances the helical stability of cagrilintide.

    In plain wordsIn lab tests, an internal bond in cagrilintide helps keep its helix shape stable.

    Peptide
    Cagrilintide
    Outcome
    Not applicableE14-R17 salt bridge
    Study

    n: not reported in source

    Cagrilintide bound to AMY1R-Gs and CTR-Gs complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    an E14-R17 intramolecular salt bridge enhancing helical stability
    1 context sentence
    Summary · context
    This study elucidates the non-selective activation mechanism by determining cryo-EM structures of Cagri bound to AMY1R-Gs and CTR-Gs complexes.

    In this study, Cagrilintide was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Cagrilintide.

  4. 05LabNot a test of Cagrilintide aloneIn vitro (cell-free)Mechanism

    In the cryo-EM structures, the C-terminal residue P37 of cagrilintide interacts with the receptor extracellular domain.

    In plain wordsIn lab tests, the last building block of cagrilintide touches the outer part of the receptor.

    Peptide
    Cagrilintide
    Outcome
    Not applicableC-terminal P37 interaction with receptor ECD
    Study

    n: not reported in source

    Cagrilintide bound to AMY1R-Gs and CTR-Gs complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    C-terminal P37Cagri interaction with the receptor ECD.
    1 context sentence
    Summary · context
    This study elucidates the non-selective activation mechanism by determining cryo-EM structures of Cagri bound to AMY1R-Gs and CTR-Gs complexes.

    In this study, Cagrilintide was a lab tool or a carrier, part of a mix, or the subject of a lab method. This result is not evidence about taking Cagrilintide.

AI wrote and checked these results. AI can make mistakes, so check important results against the source.

Version history

PepBank keeps every version of the data on this study. Status changes from Retraction Watch, Europe PMC and Crossref are listed with their source.

  1. Version 2Current

    9 Oct 2026, 18:17 UTC

    Study results updated

  2. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

Publication types

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