Introduction
Biotin peptides can be
prepared via either solid phase or solution phase, with or
without a spacer in between.
The point of biotinylation can be either sulfhydryl (SH) group or amino
group (NH2).
The covalent bond makes the attachment strong and is suitable for many
different applications.
Biotinylation
on Solid Support
While a peptide is still on solid support during the synthesis, the side chain
amino group of Lys can be available by using a special reagent, followed by a
reaction with a biotin reagent under suitable condition.
Another approach is to use biotinylated Lysine for synthesis.
Normally if the biotin can be at N-terminus, the first method is the best
to use.
If the biotin is at any position in the sequence, the second method is a
better choice.
Biotinylation
in
Solution
This method is for the peptides which are no longer on solid support.
Usually the biotin is attached to a
sulfhydryl group of Cys, for it is
more specific.
One of the advantages of using this method is that the sequence of the peptide
and the point of attachment can be identical to those conjugated to a carrier
protein, such as KLH or BSA.
Linkers
A linker can be inserted between a biotin and a peptide. It makes the biotin
more available for its affinity application. It also make the characters
of peptide less interfered by the biotin. The best linker for this purpose
is 6-aminohexanoic acid. It forms a regular peptide amide with both biotin
and peptide. It also forms a -(CH2)4- group to serve as an inert
spacer. There are other kinds of linkers for other specific applications.
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