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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)
Author(s) -
Nakamura Takahiro,
Sato Kohei,
Naruse Naoto,
Kitakaze Keisuke,
Inokuma Tsubasa,
Hirokawa Takatsugu,
Shigenaga Akira,
Itoh Kohji,
Otaka Akira
Publication year - 2016
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201600521
Subject(s) - thioester , chemistry , combinatorial chemistry , activator (genetics) , native chemical ligation , residue (chemistry) , solid phase synthesis , stereochemistry , biochemistry , cysteine , peptide , enzyme , gene
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. on page 1986 in Issue 20, 2016 (DOI: 10.1002/cbic.201600400).