Synthesis and evaluation of peptidic thrombin inhibitors bearing acid-stable sulfotyrosine analogues
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.
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)
Synthesis of Protected L-4-[Sulfono(difluoromethyl)]phenylalanine and Its Incorporation into a Peptide
matrix presented A protected form of L-4-[sulfono(difluoromethyl)]phenylalanine (F2Smp), a novel non-hydrolyzable phospho- and sulfotyrosine mimetic, was synthesized via electrophilic fluorination of a benzylic sulfonate followed by a Pd-cataly
Liu, Shifeng,Dockendorff, Chris,Taylor, Scott D.
p. 1571 - 1574
(2007/10/03)
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