Why is DMF used in peptide synthesis?
Dimethylamine is reactive toward the Fmoc protecting group and may remove it. This could result in excess couplings, and accordingly impure products. DMF is cheaper than NMP, so many peptide chemists use it in spite of its tendency to release reactive amines.
What side chains are protected by trityl in solid phase peptide synthesis?
The trityl group was recently introduced for the protection of the side chain carboxamide function of asparagine and glutamine. The 4-methyltrityl (Mtt) group, a structural modification of trityl, is presented here and allows more rapid cleavage from the protected peptides.
How do you remove Dimethylamine from DMF?
Dimethylamine degradation impurities can be removed by sparging degraded samples with an inert gas such as argon or by sonicating the samples under reduced pressure. As its name indicates, it is a derivative of formamide, the amide of formic acid. DMF is a polar (hydrophilic) aprotic solvent with a high boiling point.
Is DMF soluble in DCM?
DMF is more soluble in DCM , compared to ETOAc. Better try to extract in ETOAc or ether. DMF is soluble in cold or chilled water.
What conditions are needed to remove the Boc protecting group on the amino end?
The deprotection of a BOC-protected amine is a simple carbamate hydrolysis in acidic conditions. The starting material is dissolved in water or organic solvent, such as toluene, dichloromethane, or ethyl acetate. Concentrated hydrochloric acid, or trifluoroacetic acid (TFA) are the acids of choice.
What is amino protecting group?
The most common α-amino-protecting groups for solid-phase peptide synthesis (SPPS) are the 9-fluorenylmethoxycarbonyl (Fmoc) and the tert-butyloxycarbonyl (Boc) groups, used in the Fmoc/tert-butyl (tBu) and Boc/benzyl (Bn) strategies respectively.
What is the t-BOC Group used for in peptides?
Before the Fmoc group became popular, the t-Boc group was commonly used for protecting the terminal amine of the peptide, requiring the use of more acid stable groups for side chain protection in orthogonal strategies. Boc groups can be added to amino acids with Di-tert-butyl dicarbonate (Boc anhydride) and a suitable base.
How do you add BOC groups to amino acids?
Boc groups can be added to amino acids with Di-tert-butyl dicarbonate (Boc anhydride) and a suitable base. The t-Boc protecting group is removed by exposing the Boc-protected residue on the chain to a strong acid.
What is the importance of protecting group strategies in peptide synthesis?
Protecting group strategies are usually necessary to prevent undesirable side reactions with the various amino acid side chains. Chemical peptide synthesis most commonly starts at the carboxyl end of the peptide (C-terminus), and proceeds toward the amino-terminus (N-terminus).
How do you remove the t-BOC protecting group from a compound?
The t-Boc protecting group is removed by exposing the Boc-protected residue on the chain to a strong acid. Typical reagents of choice for deprotection in existing methods are trifluoroacetic acid (TFA) in dichloromethane, hydrochloric acid or methanesulfonic acid in dioxane.