Chemical Ligation

Researchers at Washington State University Department of Chemistry have invented an improved method of native chemical ligation. The method involves the ligation of a peptide thioacid with an aziridinyl peptide to yield an aziridinyl peptide ligation product without the use of

protecting groups. Ring opening of the ligation product ultimately yields the linearized peptide.

Advantages:

This method does not require the presence of a cysteinyl peptide for the reaction to occur and thus, it is not limited to proteins that contain or can tolerate the presence of a cysteine residue

This method is not sensitive to steric hindrance during the coupling reaction like conventional native

chemical ligation

This method results in production of unprotected peptides that are specifically modified at the

ligation sites

High product yield

All the above allow this method to be applicable for the ligation of a wide variety of molecules including peptides of any desired sequence, peptides that contain natural as well as non‐natural amino acid residues, and ones that contain various chemical modifications. The flexibility afforded by this technology enables a range of potential applications for synthetic peptides in the fields of biology and medicine.

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