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Albumin binding half-life extension: difference between revisions

Diff·revision 10 → 11·16:11, 18 Feb 2025

Difference between revision 10 and revision 11 of Albumin binding half-life extension. 2 lines changed; the page grew by 361 bytes.

Revision 10 — 23:37, 25 Jan 2025
BUD_Bertram (talk)
expand §Physical basis
4,511 bytes +110
Revision 11 — 16:11, 18 Feb 2025
ProglucagonPia (talk)
the article treated a rodent finding as human physiology; corrected
4,872 bytes +361
33The progression from the first to the second is instructive: three changes acting together produced roughly a twelvefold extension, and no single one of them would have sufficed. The terminal carboxylate of the diacid increases albumin affinity substantially; the OEG spacer holds the peptide away from the albumin surface so that receptor binding is not sterically impeded; the Aib substitution removes the [[Dipeptidyl peptidase-4|DPP-4]] cleavage site that would otherwise have become rate-limiting once renal clearance was slowed.{{r|lau2015}}33The progression from the first to the second is instructive: three changes acting together produced roughly a twelvefold extension, and no single one of them would have sufficed. The terminal carboxylate of the diacid increases albumin affinity substantially; the OEG spacer holds the peptide away from the albumin surface so that receptor binding is not sterically impeded; the Aib substitution removes the [[Dipeptidyl peptidase-4|DPP-4]] cleavage site that would otherwise have become rate-limiting once renal clearance was slowed.{{r|lau2015}}
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+35The lysine substitution is a manufacturing consideration rather than a pharmacological one. A peptide with two available lysines acylates at both, and separating the mono- and di-acylated species is a costly [[Preparative HPLC purification|preparative chromatography]] problem; substituting the unwanted lysine removes the impurity at source.{{r|knudsen2019}}
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35== References ==37== References ==
36{{reflist}}38{{reflist}}