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The solid phase now bears a dipeptide. This cycle is repeated to form the desired peptide chain. After all reactions are complete, the synthesised peptide is cleaved from the bead. The protecting groups for the amino groups mostly used in the peptide synthesis are 9-fluorenylmethyloxycarbonyl group and t-butyloxycarbonyl . A number of amino ...
The chemical synthesis of peptides can be carried out using classical solution-phase techniques, although these have been replaced in most research and development settings by solid-phase methods (see below). [3] Solution-phase synthesis retains its usefulness in large-scale production of peptides for industrial purposes moreover.
Due to the preference for a cis-amide bond [10] with the preceding residue of C2-substituted pseudoprolines, their incorporation results in a kink conformation of the peptide backbone, thus preventing peptide aggregation, self-association, or β-structure formation. Strategies for the use of Pseudoproline in Solid-Phase Peptide Synthesis (SPPS).
Combinatorial split-mix (split and pool) synthesis [12] [13] is based on the solid-phase synthesis developed by Merrifield. [14] If a combinatorial peptide library is synthesized using 20 amino acids (or other kinds of building blocks) the bead form solid support is divided into 20 equal portions.
The use of Fmoc as a temporary protecting group for amine at the N-terminus in solid phase synthesis is very widespread for Fmoc/tBu approach, because its removal with piperidine does not disturb the acid-labile linker between the peptide and the resin. [7]
The original method is based on the solid-phase synthesis of Merrifield [5] The procedure is illustrated in the figure by the flowing diagram showing of a two-cycle synthesis using the same three BBs in both cycles. Choosing the solid phase method in the S&P synthesis is reasonable since otherwise removal of the by-products from the mixture of ...
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