Amylin: difference between revisions
Diff·revision 24 → 25·16:05, 17 Sep 2025
Difference between revision 24 and revision 25 of Amylin. 3 lines changed; the page grew by 696 bytes.
| Revision 24 — 22:29, 28 Aug 2025 CuriousCallum (talk) expand §Amyloid formation 5,099 bytes ±0 | Revision 25 — 16:05, 17 Sep 2025 TirzTaxonomist (talk) move the trade-name history out of the lead and into §Regulatory history 5,795 bytes +696 | ||
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| 44 | Islet amyloid is present in the majority of pancreases examined post mortem from people with long-standing type 2 diabetes. Whether it is a cause of beta-cell loss or a consequence of prolonged secretory stress remains debated; oligomeric intermediates rather than mature fibrils are the species most often proposed as cytotoxic. | 44 | Islet amyloid is present in the majority of pancreases examined post mortem from people with long-standing type 2 diabetes. Whether it is a cause of beta-cell loss or a consequence of prolonged secretory stress remains debated; oligomeric intermediates rather than mature fibrils are the species most often proposed as cytotoxic. |
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| + | 46 | The practical consequence for peptide chemistry is that human amylin is a difficult peptide to handle: it aggregates in solution at ordinary concentrations, and any preparation of it requires attention to solvent, concentration and time. The engineered analogue pramlintide replaces three residues with prolines, which disrupts β-sheet formation and makes a stable formulation possible. Aggregation is accordingly a specification attribute for this chemistry rather than an incidental observation. See [[Peptide aggregation]].{{r|westermark2011,usp1503}} | |
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| 46 | == References == | 48 | == References == |
| 47 | {{reflist}} | 49 | {{reflist}} |
| 48 | <ref name="hay2015">Hay DL, Chen S, Lutz TA, Parkes DG, Roth JD. "Amylin: pharmacology, physiology, and clinical potential." ''Pharmacological Reviews'' 67(3):564–600 (2015). DOI:10.1124/pr.115.010629. PMID 26071095.</ref> | 50 | <ref name="hay2015">Hay DL, Chen S, Lutz TA, Parkes DG, Roth JD. "Amylin: pharmacology, physiology, and clinical potential." ''Pharmacological Reviews'' 67(3):564–600 (2015). DOI:10.1124/pr.115.010629. PMID 26071095.</ref> |
| 49 | <ref name="westermark2011">Westermark P, Andersson A, Westermark GT. "Islet amyloid polypeptide, islet amyloid, and diabetes mellitus." ''Physiological Reviews'' 91(3):795–826 (2011). DOI:10.1152/physrev.00042.2009. PMID 21742788.</ref> | 51 | <ref name="westermark2011">Westermark P, Andersson A, Westermark GT. "Islet amyloid polypeptide, islet amyloid, and diabetes mellitus." ''Physiological Reviews'' 91(3):795–826 (2011). DOI:10.1152/physrev.00042.2009. PMID 21742788.</ref> |
| + | 52 | <ref name="usp1503">United States Pharmacopeia, General Chapter <1503>, ''Quality Attributes of Synthetic Peptide Drug Substances''.</ref> | |
| 50 | <ref name="campbell2013">Campbell JE, Drucker DJ. "Pharmacology, physiology, and mechanisms of incretin hormone action." ''Cell Metabolism'' 17(6):819–837 (2013). PMID 23684623.</ref> | 53 | <ref name="campbell2013">Campbell JE, Drucker DJ. "Pharmacology, physiology, and mechanisms of incretin hormone action." ''Cell Metabolism'' 17(6):819–837 (2013). PMID 23684623.</ref> |
| 51 | 54 |