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Remove the peptide resin and dry under a high vacuum for 4 h, or preferably o/n, over KOH.Wash further with MeOH (polystyrene) or ether (polyacrylamide) to shrink the resin. Wash with DMF, acetic acid, then with DCM several times.Place the peptide resin in a sintered glass funnel and apply some suction.Method 1: Preparing peptide resin for cleavage Note: Acetic acid should not be used for washing of extremely acid-labile Rink acid, TGT, or 2-chlorotrityl resins. Thorough washing and drying must be carried out before cleavage ( Method 1).
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For PEG and polyacrylamide-based supports, washing with a mildly acidic reagent, such as acetic acid which does not cause the release of the peptide, is desirable since these types of resin tend to hold onto DMF 3. The peptide resin should be thoroughly washed, especially when DMF is used during synthesis as it is nonvolatile, and residual basic DMF can have a marked inhibitory effect on TFA-acidolysis.
#Dbz s cap 63 sub español manual
Check with the instruction manual of your synthesizer many synthesizers will automatically program the removal of the N-terminal Fmoc-group as a last step in the synthesis. Nevertheless, as a general, non-malodorous cleavage cocktail, this mixture has proved remarkably effective.įor those who do not wish to use the recommendations given in Table 1, the flow-chart shown in Figure 1 will aid in the selection of the most appropriate mixture.īefore acid cleavage of the peptidyl resin can be performed, the N-terminal Fmoc group must be removed using piperidine.
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There are, of course, sequences, especially those which contain cysteine and numerous t-butyl protected residues, for which this mixture does not give satisfactory results in these cases, the addition of EDT to the mixture or the use of reagent K is recommended. If these recommendations are followed, the use of TFA/TIS/water (95:2.5:2.5) will suffice for most sequences. Most problems can be ameliorated by the appropriate choice of protected amino acid derivative and resin ( Table 1). However, advances in protecting group and linker technology, particularly the introduction of Fmoc-Trp(Boc) and Fmoc-Arg(Pmc/Pbf) derivatives, such complex mixtures containing toxic and malodorous reagents are no longer necessary, except in exceptional circumstances. Many universal cleavage mixtures have been advocated, the most popular of which is Reagent K (TFA/water/phenol/thioanisole/EDT ) 1. To prevent this, various nucleophilic reagents (known as scavengers) are added to the TFA to quench these ions 1, 2 During this process, highly reactive cationic species are generated from the protecting groups and the handles on the resin, and these can, unless trapped, react with, and hence modify, those residues which contain nucleophilic functional groups: Trp, Met, Tyr, and Cys. In Fmoc SPPS, this step is normally carried out by treating the peptidyl resin with TFA. Having successfully synthesized a protected peptide, one is confronted with a difficult task of having to simultaneously detach the peptide from the resin support and remove all the side-chain protecting groups of the amino acid residues to yield the desired peptide.