Chemical Synthesis of Biologically Active Monoglycosylated GM2‐Activator Protein Analogue Using  N ‐Sulfanylethylanilide Peptide | Zendy

Sato Kohei | Zendy; Shigenaga Akira | Zendy; Kitakaze Keisuke | Zendy; Sakamoto Ken | Zendy; Tsuji Daisuke | Zendy; Itoh Kohji | Zendy; Otaka Akira | Zendy

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Chemical Synthesis of Biologically Active Monoglycosylated GM2‐Activator Protein Analogue Using N ‐Sulfanylethylanilide Peptide

Author(s) -

Sato Kohei,

Shigenaga Akira,

Kitakaze Keisuke,

Sakamoto Ken,

Tsuji Daisuke,

Itoh Kohji,

Otaka Akira

Publication year - 2013

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.201303390

Subject(s) - native chemical ligation , peptide , activator (genetics) , computer science , chemistry , fragment (logic) , chemical synthesis , glycoprotein , computational biology , combinatorial chemistry , biochemistry , stereochemistry , biology , algorithm , gene , in vitro

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.

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