Synfacts 2019; 15(05): 0573
DOI: 10.1055/s-0037-1612446
Peptide Chemistry
© Georg Thieme Verlag Stuttgart · New York

Synthesis of Peptides by Using Recombinant Proteins

Hisashi Yamamoto
Manthena Chaithanya
Kawakami T, Akaji K, Aimoto S. * Osaka University, Japan
Peptide Bond Formation Mediated by 4,5-Dimethoxy-2-mercaptobenzylamine after Periodate Oxidation of the N-Terminal Serine Residue.

Org. Lett. 2001;
3: 1403-1405
Further Information

Publication History

Publication Date:
15 April 2019 (online)



In 2001, Aimoto and co-workers reported an approach for the synthesis of polypeptides by using recombinant proteins in combination with peptide thioesters. A thiol-linker-attached peptide for condensation with the peptide thioester was successfully synthesized from a nonprotected peptide through periodate oxidation of an N-terminal serine residue, followed by reductive amination with 4,5-dimethoxy-2-mercaptobenzylamine (Dmmb-NH2).



A N-2-mercaptobenzyl group on the backbone of a peptide is too stable under acidic conditions. The introduction of two methoxy groups on the benzene ring permitted the Dmmb group to be removed, after condensation, by treatment with 1 M TfOH in TFA. Instead of periodate oxidation of serine and threonine, transamination of N-terminal amino groups could also be used in principle, although the stereochemistry resulting from the reductive amination should be controlled.