Amylin receptor agonist: difference between revisions
Diff·revision 4 → 5·05:37, 9 Nov 2024
Difference between revision 4 and revision 5 of Amylin receptor agonist. 2 lines changed; the page grew by 308 bytes.
| Revision 4 — 13:00, 25 Oct 2024 RedirectRini (talk) expand §Analytical notes 2,228 bytes +627 | Revision 5 — 05:37, 9 Nov 2024 MolarMassMaeve (talk) fix a dangling clause 2,536 bytes +308 | ||
|---|---|---|---|
| 10 | Two generations exist. Pramlintide, approved in 2005 as an adjunct to insulin, substitutes three prolines into the human sequence to disrupt β-sheet formation; its short half-life requires injection at each meal, which limited uptake. [[Cagrilintide|Cagrilintide]] is a long-acting analogue employing [[Albumin binding half-life extension|acylation]] for weekly dosing and is under development principally in combination with [[Semaglutide|semaglutide]] as [[CagriSema|CagriSema]].{{r|lau2021}} | 10 | Two generations exist. Pramlintide, approved in 2005 as an adjunct to insulin, substitutes three prolines into the human sequence to disrupt β-sheet formation; its short half-life requires injection at each meal, which limited uptake. [[Cagrilintide|Cagrilintide]] is a long-acting analogue employing [[Albumin binding half-life extension|acylation]] for weekly dosing and is under development principally in combination with [[Semaglutide|semaglutide]] as [[CagriSema|CagriSema]].{{r|lau2021}} |
| 11 | 11 | ||
| + | 12 | The clinical interest in the class rests on the observation that amylin-mediated satiety is mechanistically distinct from [[Satiety signalling|GLP-1-mediated satiety]] and appears additive to it, so that a combination produces more weight loss than either component alone at the doses studied.{{r|lau2021}} | |
| + | 13 | ||
| 12 | == Design == | 14 | == Design == |
| 13 | The problem to be solved is amyloidogenicity. Human amylin forms cross-β fibrils at concentrations well below those needed for a pharmaceutical formulation, and a peptide that aggregates in the vial is not a medicine.{{r|hay2015}} | 15 | The problem to be solved is amyloidogenicity. Human amylin forms cross-β fibrils at concentrations well below those needed for a pharmaceutical formulation, and a peptide that aggregates in the vial is not a medicine.{{r|hay2015}} |