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Orforglipron: difference between revisions

Diff·revision 2 → 3·10:49, 3 Dec 2024

Difference between revision 2 and revision 3 of Orforglipron. 5 lines changed; the page grew by 781 bytes.

Revision 2 — 10:24, 22 Nov 2024
SemaglutideSasha (talk)
British spelling per PP:MOS
1,574 bytes ±0
Revision 3 — 10:49, 3 Dec 2024
RetatrutideRuben (talk)
reorder the analogues chronologically rather than alphabetically
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11Small-molecule agonism at a class B G-protein-coupled receptor was long considered difficult, because the natural ligand engages a large surface across two receptor domains.{{r|graaf2016}} Orforglipron binds a pocket near the extracellular face of the transmembrane bundle and stabilises an active conformation without reproducing the peptide's binding mode.{{r|kawai2020}}11Small-molecule agonism at a class B G-protein-coupled receptor was long considered difficult, because the natural ligand engages a large surface across two receptor domains.{{r|graaf2016}} Orforglipron binds a pocket near the extracellular face of the transmembrane bundle and stabilises an active conformation without reproducing the peptide's binding mode.{{r|kawai2020}}
1212
+13== Molecular basis ==
+14The receptor's orthosteric peptide site is a poor target for a small molecule: the natural ligand contacts both the extracellular domain and the transmembrane bundle across a large interface, and a molecule of a few hundred daltons cannot reproduce that. Orforglipron instead occupies a pocket accessible from the extracellular face of the bundle and acts as an agonist by stabilising the same active receptor conformation by a different route.{{r|kawai2020}}
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+16A consequence is species selectivity. The pocket differs between human and rodent receptors sufficiently that activity does not translate, and preclinical work required humanised receptor models — a practical complication of small-molecule work at this target that peptide agonists do not face.
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13== References ==18== References ==
14{{reflist}}19{{reflist}}