Peptide Chemistry STP


Structure of the Rnd3 C-terminal farnesylated phosphopeptide

Structure of the Rnd3 C-terminal farnesylated phosphopeptide bound to 14-3-3ζ shown with the SIGMAA-weighted 2Fo − Fc electron density omit map (σ = 1.0).

We make peptides for Crick researchers for use in experiments to study how biomolecules such as proteins interact with each other. 

Each peptide is as unique as its sequence and many of the peptides we make are long and highly modified. 

Modifications include dye-labelled, lipidated, branched, cyclic and disulphide-bridged peptides. 

Some peptides require solution phase chemistry or manual synthesis such as peptides with a hydrocarbon bridge to constrain their secondary structure, peptides designed to crosslink with one another and very long peptides made in sections and ligated together.

We analyse all peptides by high-pressure liquid chromatography (HPLC) and mass spectroscopy and purify peptides using reverse phase chromatographic methods.