Albumin binding half-life extension: difference between revisions
Diff·revision 17 → 18·07:44, 27 Aug 2025
Difference between revision 17 and revision 18 of Albumin binding half-life extension. 2 lines changed; the page grew by 378 bytes.
| Revision 17 — 08:45, 26 Jul 2025 HalfLifeHavel (talk) expand §Physical basis 6,021 bytes ±0 | Revision 18 — 07:44, 27 Aug 2025 GIP_Genoveva (talk) add the citation for the co-secretion finding 6,399 bytes +378 | ||
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| 40 | They also self-associate. Acylated incretin analogues form oligomers in concentrated solution, which is part of what stabilises the marketed formulations but which complicates [[Peptide aggregation|aggregation]] assessment: an apparent high-molecular-weight species may be a reversible oligomer rather than an irreversible aggregate, and size-exclusion chromatography under dissociating and non-dissociating conditions will disagree.{{r|ich_q6b}} | 40 | They also self-associate. Acylated incretin analogues form oligomers in concentrated solution, which is part of what stabilises the marketed formulations but which complicates [[Peptide aggregation|aggregation]] assessment: an apparent high-molecular-weight species may be a reversible oligomer rather than an irreversible aggregate, and size-exclusion chromatography under dissociating and non-dissociating conditions will disagree.{{r|ich_q6b}} |
| 41 | 41 | ||
| + | 42 | For anyone comparing a [[Certificate of analysis|certificate]] on an acylated peptide against one on an unmodified peptide, the practical point is that the chromatographic conditions are not transferable and a method that resolves one will not necessarily resolve the other. A certificate that does not name its gradient and column cannot be checked for adequacy.{{r|usp1503}} | |
| + | 43 | ||
| 42 | == References == | 44 | == References == |
| 43 | {{reflist}} | 45 | {{reflist}} |