Chemical Synthesis of Biologically Active Monoglycosylated GM2‐Activator Protein Analogue Using N‐Sulfanylethylanilide Peptide1. Issue 30 (13th June 2013)

• Record Type: Journal Article
• Authors: Sato, Kohei; Shigenaga, Akira; Kitakaze, Keisuke; Sakamoto, Ken; Tsuji, Daisuke; Itoh, Kohji; Otaka, Akira
• Is Part Of: Angewandte Chemie international edition. Volume 52:Issue 30(2013)
• Page Start: 7855
• Page End: 7859
• Publication Date: 2013-06-13
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.201303390
• Languages: English
• ISSNs: 1433-7851

Abstract

<abstract abstract-type="graphical" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p> <bold>Going to SEA(lide)</bold>: 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 <italic>N</italic>‐sulfanylethylanilide (SEAlide) peptides in the kinetic chemical ligation synthesis of a large peptide fragment, and a convergent native chemical ligation for final fragment assembly.<boxed-text content-type="graphic" position="anchor" orientation="portrait"><graphic position="anchor" mimetype="image" xlink:href="ark:/27927/pgg270w4b26" orientation="portrait" xlink:type="simple" xmlns:xlink="http://www.w3.org/1999/xlink" /></boxed-text></p> </abstract>