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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.