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Study · Not a test of the peptide alone · 2025

2 results

Structural and dynamic features of cagrilintide binding to calcitonin and amylin receptors.

Cao J, Belousoff MJ, Johnson RM, Keov P, Mariam Z, Deganutti G, Christopoulos G, Hick CA, Reedtz-Runge S, Glendorf T, Ballarín-González B, Raun K, Bayly-Jones C, Wootten D, Sexton PM

Nature communications10 Apr 2025Cited by 16 (Europe PMC)

PMID40204768 (opens in a new tab)PMCIDPMC11982234 (opens in a new tab)DOI10.1038/s41467-025-58680-y (opens in a new tab)PepBankPUB-40204768
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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: CC BY-NC-ND. Results still quote short attributed sentences.

Results from this study2

No result from this study comes from a test of the peptide.

Studies that did not test the peptide alone2

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. 01LabNot a test of Cagrilintide aloneIn vitro (cell-free)Mechanism

    Structures show that cagrilintide has an amylin-like binding mode at AMY1R, AMY2R, AMY3R and the calcitonin receptor.

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

    Peptide
    Cagrilintide
    Outcome
    Not applicableBinding mode at amylin and calcitonin receptors
    Study

    n: not reported in source

    Cagrilintide-bound active AMY1R, AMY2R, AMY3R and CTR complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    These data reveal that cagrilintide has an amylin-like binding mode
    1 context sentence
    Summary · context
    Here, we determine structures of cagrilintide bound to Gs-coupled, active, amylin receptors (AMY1R, AMY2R, AMY3R) and calcitonin receptor (CTR) and compare cagrilintide interactions and the dynamics of receptor complexes with previously reported structures of recepto…

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

    Compared with other peptides, cagrilintide induces distinct conformational dynamics at calcitonin-family receptors.

    In plain wordsIn lab tests, cagrilintide changed the movement of calcitonin-family receptors differently from other peptides.

    Peptide
    Cagrilintide
    Outcome
    Not applicableReceptor conformational dynamics
    Study

    n: not reported in source

    Cagrilintide-bound active AMY1R, AMY2R, AMY3R and CTR complexes
    Outcome group
    Receptor activity and mechanism · Pharmacology

    Source sentences

    Summary
    but, compared to other peptides, induces distinct conformational dynamics at calcitonin-family receptors that could contribute to its clinical efficacy.
    1 context sentence
    Summary · context
    Here, we determine structures of cagrilintide bound to Gs-coupled, active, amylin receptors (AMY1R, AMY2R, AMY3R) and calcitonin receptor (CTR) and compare cagrilintide interactions and the dynamics of receptor complexes with previously reported structures of recepto…

    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 3Current

    27 Oct 2026, 16:35 UTC

    Study data updated · source update from Europe PMC

  2. Version 2

    9 Oct 2026, 18:17 UTC

    Study results updated

  3. Version 1

    9 Oct 2026, 03:04 UTC

    First added · source update from Europe PMC

Subjects

Terms as the source lists them.

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