282734-33-2Relevant academic research and scientific papers
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
, 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.
Synthesis of selenocysteine-containing dipeptides modeling the active site of thioredoxin reductase
Shimodaira, Shingo,Iwaoka, Michio
, 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.
Stereospecific synthesis of a carbene-generating angiotensin II analogue for comparative photoaffinity labeling: Improved incorporation and absence of methionine selectivity
Pillion, Dany,Dera?t, Maud,Holleran, Brian J.,Escher, Emanuel
, p. 2200 - 2209 (2007/10/03)
A stereospecific convergent synthesis of N-[(9-fluorenyl)methoxycarbonyl]- p-[3-(trifluoromethyl)-3H-diazirin-3-yl]-L-phenylalanine (Fmoc-12, Fmoc-Tdf) and its incorporation into the C-terminal position of the angiotensin II (AngII) peptide to form 125I[Sar1,Tdf8]AngII ( 125I-13) is presented. This amino acid photoprobe is a highly reactive carbene-generating diazirine phenylalanine derivative that can be used for photoaffinity labeling. Using model receptors, we compared the reactivity and the Met selectivity of 12 to that of the widely used and reputedly Met-selectivep-benzoyl-L-phenylalanine (Bpa) photoprobe. Wild-type and mutant AngII type 2 receptors, a G protein-coupled receptors, were photolabeled with 125I-13 as well as with 125I-[Sar1,Bpa 8]AngII (125I-14), and the respective incorporation yields were assessed. The carbene-generating 12 was more reactive toward inert residues and was not Met-selective compared to the biradical ketone-generating Bpa, allowing for more precise determination of ligand contact points in peptidergic receptors.
