Learn a little about peptides every day--1

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Fmoc peptide synthesis -- Solid Bio. Fmoc chemistry was developed by Eric Atherton and Bob Sheppard in the late 1970s at the Molecular Biology Laboratory at Cambridge University, and was reviewed by Chan and White (\"Fmoc Solid-Phase Peptide Synthesis: A Practical Method\", Oxford University Press, 2000). In Fmoc solid-phase peptide synthesis, the peptide chain is built up step by step, with one amino acid added at a time, while being attached to an insoluble resin carrier. This allows the removal of reaction by-products through simple washing at each step. The amino acid is protected at its amino terminus by an Fmoc (9-fluorenylmethoxycarbonyl) group, and after activation at its carboxylic acid terminus, it is coupled to the growing chain. Then, the Fmoc group is removed through **treatment, and the process is repeated. After peptide assembly is complete, it can be removed from the resin by treatment with trifluoroacetic acid (TFA). At the same time, the protecting groups on the amino acid side chains were also removed, yielding a crude linear peptide. One-step purification by reverse-phase HPLC is usually sufficient to obtain peptides with a purity > 95%. The Fmoc synthesis reaction is mild, flexible, and widely applicable, thus offering more synthetic options than alternative Boc-based methods. For example, TFA is used only once during the cleavage process, whereas in the Boc process it is used in each cycle.