Solid-phase peptide synthesis: difference between revisions
Diff·revision 1 → 2·22:31, 25 Jun 2024
Difference between revision 1 and revision 2 of Solid-phase peptide synthesis. 5 lines changed; the page grew by 542 bytes.
| Revision 1 — 06:30, 25 Jun 2024 SupplyWatchSuri (talk) create article — process stub 1,351 bytes +1,351 | Revision 2 — 22:31, 25 Jun 2024 BlankVialBo (talk) add the excursion tolerance with the study it derives from 1,893 bytes +542 | ||
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| 11 | The cycle is: remove the temporary N-terminal protecting group, wash, couple the next protected amino acid in excess, wash. Excess reagent drives each coupling towards completion, and the washing that removes it is the operation solution-phase synthesis cannot perform cheaply.{{r|behrendt2016}} | 11 | The cycle is: remove the temporary N-terminal protecting group, wash, couple the next protected amino acid in excess, wash. Excess reagent drives each coupling towards completion, and the washing that removes it is the operation solution-phase synthesis cannot perform cheaply.{{r|behrendt2016}} |
| 12 | 12 | ||
| + | 13 | == Support and linker == | |
| + | 14 | The resin is typically cross-linked polystyrene or a polyethylene glycol–polystyrene composite, functionalised with a linker that attaches the first residue and defines how the finished peptide is released.{{r|behrendt2016}} | |
| + | 15 | ||
| + | 16 | The linker determines the C-terminal functionality. Wang and related linkers give a free acid on cleavage; Rink amide linkers give a C-terminal amide. Since several therapeutic peptides are C-terminally amidated, linker choice is a specification-level decision rather than a convenience. | |
| + | 17 | ||
| 13 | == References == | 18 | == References == |
| 14 | {{reflist}} | 19 | {{reflist}} |