27918-31-6Relevant articles and documents
Exploring new activating groups for reactive cysteine NCAs
Huesmann, David,Sch?fer, Olga,Braun, Lydia,Klinker, Kristina,Reuter, Thomas,Barz, Matthias
, p. 1138 - 1142 (2016/03/09)
Due to its ability to reversibly crosslink proteins, cysteine has a unique role as an amino acid in nature. For controlled, asymmetric formation of disulfides from two thiols, one thiol needs to be activated. While few activating groups for cysteine have been proposed, they are usually not stable against amines making them unsuitable for solid phase peptide synthesis or amine initiated polymerization of α-amino acid-N-carboxy-anhydrides (NCAs). In this Letter we describe a series of new thiol activated cysteines, as well as their NCAs and explore the link between electron deficiency of the leaving group and control over NCA polymerization.
THIOL-PROTECTED AMINO ACID DERIVATIVES AND USES THEREOF
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Page/Page column 43, (2015/11/27)
The present invention relates to thiol-protected amino acid derivatives of formulae (I) and (II), peptides and block-copolymers containing the compounds and methods for preparing same. The present invention also relates to core-shell particles comprising such thiol-protected block-copolymers and compositions thereof.
Organofluorine sulfur-containing compounds: V. Joint pyrolysis with chlorine or bromine of polyfluoroarenethioles, polyfluorohetarenethioles, and their derivatives
Platonov,Maksimov,Dvornikova,Nikul'shin
, p. 1647 - 1653 (2007/10/03)
Joint pyrolysis with chlorine and bromine of polyfluoroarenethiols, -hetarenethiols, and their derivatives at 300-650°C furnished polyfluorocompounds containing chlorine and bromine. 2005 Pleiades Publishing, Inc.