76587-61-6Relevant articles and documents
Synthesis of selenocysteine-containing dipeptides modeling the active site of thioredoxin reductase
Shimodaira, Shingo,Iwaoka, Michio
supporting information, p. 750 - 752 (2019/04/26)
Four cyclic dipeptides modeling the active site of thioredoxin reductase (TrxR), UU, CU, UC, and CC, where U and C represent selenocystine and cystine, respectively, were synthesized and their glutathione peroxidase (GPx)-like catalytic activity was evaluated by the reaction of hydrogen peroxide (H2O2) with glutathione (GSH) in the presence of glutathione reductase (GR). Among these, only UC exhibited the significant antioxidant capacity, suggesting that an atomic environment around the Se–S bond is relevant to the reactivity toward a thiol substrate.
Investigation of Cysteine as an Activator of Side-Chain N→S Acyl Transfer and Tail-to-Side-Chain Cyclization
Castillo-Pazos, Durbis J.,Macmillan, Derek
, p. 1923 - 1928 (2017/09/13)
N→S Acyl transfer is a popular method for the postsynthesis production of peptide C α -thioesters for use in native chemical ligation and for the synthesis of head-to-tail cyclic peptides. Meanwhile thioester formation at the side chain of aspartic or glutamic acids, leading to tail-to-side-chain-cyclized species, is less common. Herein we explore the potential for cysteine to function as a latent thioester when appended to the side chain of glutamic acid. Initial insights gained through study of C-terminal β-alanine as a model for the increased chain length were ultimately applied to peptide macrocyclization. Our results emphasize the increased barrier to acyl transfer at the glutamic acid side chain and indicate how a slow reaction, facilitated by cysteine itself, may be accelerated by fine-tuning of the stereoelectronic environment..
Carbohydrate-based VEGF inhibitors
Haag, Tobias,Hughes, Richard A.,Ritter, Gerd,Schmidt, Richard R.
, p. 6016 - 6033 (2008/09/17)
Cyclic peptide-carbohydrates (compounds 1a-c, 2, 33, 34) were designed and synthesized to act as mimetics of loop 2 of the proangiogenic molecule vascular endothelial growth factor D (VEGF-D). The mimetics were designed to inhibit dimerization of the receptors (VEGFR-2 and VEGFR-3) by VEGF-D, and thus have the potential to inhibit angiogenesis. To this end, in the previously described cyclic octapeptide CNEESLIC and the cyclic nonapeptide CGNEESLIC inhibitors derived from VEGF-D loop 2, the NEES tetrapeptide residue was replaced by a carbohydrate scaffold having the amino acid side chain mimics in positions proposed by modeling studies. Attachment of the additional amino acids using the Fmoc technology, then formation of the cyclic disulfides, and finally total deprotection afforded the target molecules of which 2 and 34 showed an ability to inhibit the biological activity of VEGF-D through VEGFR-2 in cell-based assays, albeit at high mimetic concentration. Wiley-VCH Verlag GmbH & Co. KGaA, 2007.