Solid Phase

Peptide Synthesis (SPPS)

Solid phase peptide synthesis (SPPS) was first described by Robert B. Merrifield in 1963. For this cost-efficient method that has considerably contributed to the success of peptides, for example, in drug discovery or biomaterials research, Merrifield was awarded the Nobel Prize in 1984. The main feature as compared to solution phase synthesis is a massive reduction of purification steps, resulting in significant time savings, particularly in the production of larger peptides.

The most common SPPS strategies are performed from the C-terminal to the N-terminal amino acid. The first step is the attachment of the C-terminal amino acid to a solid support, which is an insoluble and porous, functionalized resin. Prior to each coupling step, each amino acid must be protected to avoid side reactions.

As a pioneer in manufacturing protected amino acid building blocks, SENN has developed outstanding experience in producing compounds for SPPS including Fmoc- or Boc-protected amino acids.

By coupling protected amino acids in a successive manner, an elongated chain of amino acids is formed. This technique allows for the rapid formation of peptide chains through stepwise reactions of amino acid derivatives on the inert resin. During the entire synthesis the peptide remains covalently bound to the resin, while reagents and by-products can be carefully removed by filtration and washing. As compared to the solution phase synthesis, time-consuming isolation of an intermediate after each reaction step is not necessary. At the end of each synthesis, the crude peptide is cleaved from the resin, followed by purification if needed.

Using our extensive knowledge and flexible capabilities, we determine the most efficient purification strategy, for example, recrystallization or preparative HPLC.