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. 2013 Jul 22;52(30):7855-9.
doi: 10.1002/anie.201303390. Epub 2013 Jun 13.

Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide

Kohei Sato  1 , Akira Shigenaga, Keisuke Kitakaze, Ken Sakamoto, Daisuke Tsuji, Kohji Itoh, Akira Otaka
Affiliations

Chemical synthesis of biologically active monoglycosylated GM2-activator protein analogue using N-sulfanylethylanilide peptide

Kohei Sato et al. Angew Chem Int Ed Engl. .

Abstract

Going to SEA(lide): Total chemical synthesis of a 162-residue glycoprotein analogue of the monoglycosylated human GM2-activator protein (GM2AP) was achieved. Key steps were the use of N-sulfanylethylanilide (SEAlide) peptides in the kinetic chemical ligation synthesis of a large peptide fragment, and a convergent native chemical ligation for final fragment assembly.

Keywords: glycoproteins; glycosylation; peptides; solid-phase synthesis; synthesis design.

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