Chemists commonly attempt to make peptides via \"solid-phase synthesis\". In thi

Question

Chemists commonly attempt to make peptides via "solid-phase synthesis". In this technique, the terminal amino acid is attached to a solid bead with the amino group exposed. A subsequent amino acid is added and allowed to react, thus extending the peptide. This second amino acid, and the subsequent ones, contain a protecting group (PG) on the amino functional group. After each amino acid is added, the protecting group must be removed before adding the next one. Explain why this technique is important and superior to simply mixing all the amino acids simultaneously. a) Show 2 examples of what could occur if a scientist were to attempt synthesizing seryl-glutaminyl-alanine w/out using this technique.

Explanation / Answer

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Solid-phase synthesis is a method in which molecules are bound on a bead and can be synthesized the target molecule step-by-step. Compared with normal synthesis in a liquid state, it is easier to remove excess reactant or byproduct from the product.

In this method, building blocks are protected at all reactive functional groups. The two functional groups will be able to participate in the desired reaction on the bead can be controlled by the order of deprotection.

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