3-硝基-2-吡啶硫酰氯

Int. J. Pept. Protein Res. 43(4) , 363-6, (1994)

The 3-nitro-2-pyridinesulphenyl (Npys) moiety is finding increasing utility as a protecting-activating group for cysteine, particularly in the synthesis of cyclic and unsymmetrical disulfides using the Boc strategy. This chemistry has been extended to peptide...

Int. J. Pept. Protein Res. 42(2) , 159-64, (1993)

3-Nitro-2-pyridinesulfenyl chloride (NpysCl) is the starting material for the synthesis of N-, O- and S-Npys-protected amino acids. Two efficient, novel synthetic routes to NpysCl are described. The stability of NpysCl was determined in a variety of solvents,...

J. Chromatogr. A. 597(1-2) , 425-8, (1992)

The thiol groups of leucinthiol, cysteamine and cysteine incorporated into opioid peptides enkephalin and morphiceptin were activated by the 3-nitro-2-pyridinesulphenyl (Npys) group to form mixed disulphides highly reactive to a free thiol. Enkephalin analogu...

Pept. Res. 5(5) , 262-4, (1992)

Two recent reports on the partial lability of the 3-nitro-2-pyridinesulfenyl (Npys) thiol protecting group towards 1-hydroxy-benzotriazole (HOBt) have prompted a rechecking of the chemical behavior of this group. Using both soluble and polymer-bound forms of ...

Int. J. Pept. Protein Res. 35(6) , 545-9, (1990)

The hydroxylic side-chain functional groups of serine, threonine, hydroxproline and tyrosine, the alpha and epsilon-amino moieties of lysine and the thiol group of cysteine were masked by the 3-nitro-2-pyridinesulfenyl (Npys) protecting group. Deprotection wa...

Pept. Res. 7 , 32-35, (1994)

Thrombin-induced platelet aggregation has been suggested to play an important role in reocclusion following thrombolytic therapy or angioplasty for treatment of myocardial infarction. We previously demonstrated that thrombin-induced platelet aggregation is in...

Int. J. Pept. Protein Res. 45(2) , 173-9, (1995)

TASPs (template-assembled synthetic peptides) are generated by the covalent attachment of linear peptides to a common peptide backbone, thus generating larger synthetic peptides/proteins with prefolded structure. In this work we present a strategy for the syn...

Biochem. Biophys. Res. Commun. 355(4) , 1000-5, (2007)

The inhibitory capacity of C-Npys (S-[3-nitro-2-pyridinesulfenyl]) derivatives over thiol-containing serine proteases has never been tested. In the present work we used an extracellular serine-thiol proteinase activity from the fungal pathogen Paracoccidioide...