110797-35-8Relevant articles and documents
Synthesis of the antimicrobial S-Linked glycopeptide, glycocin F
Brimble, Margaret A.,Edwards, Pat J.,Harris, Paul W. R.,Norris, Gillian E.,Patchett, Mark L.,Wright, Tom H.,Yang, Sung-Hyun,Carley, Sarah E.
, p. 3556 - 3561 (2015)
The first total synthesis of glycocin F, a uniquely diglycosylated antimicrobial peptide bearing a rare S-linked N-acetylglucosamine (GlcNAc) moiety in addition to an O-linked GlcNAc, has been accomplished using a native chemical ligation strategy. The synthetic and naturally occurring peptides were compared by HPLC, mass spectrometry, NMR and CD spectroscopy, and their stability towards chymotrypsin digestion and antimicrobial activity were measured. This is the first comprehensive structural and functional comparison of a naturally occurring glycocin with an active synthetic analogue.
Synthesis of selenocysteine-containing dipeptides modeling the active site of thioredoxin reductase
Shimodaira, Shingo,Iwaoka, Michio
, p. 750 - 752 (2019)
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.
Synthesis and evaluation of peptidic thrombin inhibitors bearing acid-stable sulfotyrosine analogues
Agten, Stijn M.,Calisto, Bárbara M.,Dowman, Luke J.,Payne, Richard J.,Pereira, Pedro José Barbosa,Ripoll-Rozada, Jorge
supporting information, p. 10923 - 10926 (2021/10/22)
Tyrosine sulfation is an important post-translational modification of peptides and proteins which underpins and modulates many protein-protein interactions. In order to overcome the inherent instability of the native modification, we report the synthesis of two sulfonate analogues and their incorporation into two thrombin-inhibiting sulfopeptides. The effective mimicry of these sulfonate analogues for native sulfotyrosine was validated in the context of their thrombin inhibitory activity and binding mode, as determined by X-ray crystallography.
