Back Cover: Tailored Synthesis of 162‐Residue S‐Monoglycosylated GM2‐Activator Protein (GM2AP) Analogues that Allows Facile Access to a Protein Library (ChemBioChem 20/2016). (30th September 2016)

• Record Type: Journal Article
• Authors: Nakamura, Takahiro; Sato, Kohei; Naruse, Naoto; Kitakaze, Keisuke; Inokuma, Tsubasa; Hirokawa, Takatsugu; Shigenaga, Akira; Itoh, Kohji; Otaka, Akira
• Is Part Of: Chembiochem. Volume 17:Number 20(2016)
• Page Start: 1994
• Page End: 1994
• Publication Date: 2016-09-30
• Subjects: chemoselectivity -- GM2AP -- kinetically controlled ligation -- native chemical ligation -- protein modifications; Biochemistry -- Periodicals; Molecular biology -- Periodicals; Pharmaceutical chemistry -- Periodicals; 572
• DOI: 10.1002/cbic.201600521
• Languages: English
• ISSNs: 1439-4227

Abstract

Abstract : The back cover picture shows a tailored synthesis of 162‐residue S‐monoglycosylated GM2‐activator protein (GM2AP) analogues. N ‐Sulfanylethylanilide (SEAlide), as a crypto‐thioester, and prolyl thioester peptides were successfully used in kinetically controlled ligation protocols. Tailored synthesis featuring the use of such kinetically controlled ligations allows facile access to a protein library of GM2AP analogues. More information can be found in the full paper by A. Otaka et al. onpage 1986 in Issue 20, 2016 (DOI:10.1002/cbic.201600400 ).