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Biotinylation is a widely applied modification in life sciences research. The biotin moiety has a very strong affinity for streptavidin (Kd < 10-10 M) and biotinylation of peptides is therefore an efficient method to specifically bind peptides to streptavidin coated surfaces.
Biotinylation of peptides can be performed either at the N- or C-terminus. Biotinylation at the N-terminus can be performed directly to the primary-terminal amino group, whereas biotinylation is usually performed at the ε-amino group of an (extra) C-terminal lysine.
In case the distance between the biotin unit and the peptide is important, for instance to avoid sterical hindrance, a linker can be inserted between biotin and the peptide sequence. The 6-carbon ε-aminocaproic (Ahx) is a popular spacer; however, other spacers can also be applied based upon specific requirement.