17035-90-4

Usage

Chemical Properties

mp 180-190°C[a]D 10.5° (c=4, water)

Brand name

Targinine is BAN.

InChI:InChI=1/C7H16N4O2.C2H4O2/c1-10-7(9)11-4-2-3-5(8)6(12)13;1-2(3)4/h5H,2-4,8H2,1H3,(H,12,13)(H3,9,10,11);1H3,(H,3,4)/t5-;/m0./s1

Upstream product

• 3184-13-2 L-ornithine hydrochloride 
• 44387-05-5 S-methyl-N-methyl-isothiourea 
• 2640-58-6 Nα-benzyloxycarbonyl-L-ornithine 
• 74-79-3 L-arginine 
• 14031-35-7 S-Adenosyl-L-methionine 
• 25693-00-9 (S)-2-Amino-5-{[1-phenyl-meth-(Z)-ylidene]-amino}-pentanoic acid 
• 506-68-3 bromocyane 
• 70-26-8 L-ornithine 
• 74-89-5 methylamine 
• 134810-05-2 N-α-carbobenzyloxy-N^G-methyl-(L)-arginine 
• 41306-45-0 N,S-dimethylisothiourea hydroiodide 

Relevant academic research and scientific papers

Binding Methylarginines and Methyllysines as Free Amino Acids: A Comparative Study of Multiple Host Classes**

Methylated free amino acids are an important class of targets for host-guest chemistry that have recognition properties distinct from those of methylated peptides and proteins. We present comparative binding studies for three different host classes that are each studied with multiple methylated arginines and lysines to determine fundamental structure-function relationships. The hosts studied are all anionic and include three calixarenes, two acyclic cucurbiturils, and two other cleft-like hosts, a clip and a tweezer. We determined the binding association constants for a panel of methylated amino acids using indicator displacement assays. The acyclic cucurbiturils display stronger binding to the methylated amino acids, and some unique patterns of selectivity. The two other cleft-like hosts follow two different trends, shallow host (clip) following similar trends to the calixarenes, and the other more closed host (tweezer) binding certain less-methylated amino acids stronger than their methylated counterparts. Molecular modelling sheds some light on the different preferences of the various hosts. The results identify hosts with new selectivities and with affinities in a range that could be useful for biomedical applications. The overall selectivity patterns are explained by a common framework that considers the geometry, depth of binding pockets, and functional group participation across all host classes.

Two-Enzyme Pathway Links l-Arginine to Nitric Oxide in N-Nitroso Biosynthesis

Nitric oxide (NO) has wide-ranging roles in biology, but less is known about its role in building chemical diversity. Here we report a new route to NO from the biosynthetic pathway to the N-nitroso compound streptozocin. We show that the N-nitroso group of streptozocin comes from the biosynthetic reassembly of l-arginine, with the guanidino nitrogens forming a nitrogen-nitrogen bond. To understand this biosynthetic process, we identify the biosynthetic gene cluster of streptozocin and demonstrate that free l-arginine is N-methylated by StzE to give N?‰-monomethyl-l-arginine. We show that this product is then oxidized by StzF, a nonheme iron-dependent enzyme unrelated to known nitric oxide synthases, generating a urea compound and NO. Our work implies that formation and capture of NO is the likely route to N-nitroso formation in vivo. Altogether, our work unveils a new enzyme pair for the production of NO from l-arginine and sets the stage for understanding biosynthetic routes to N-nitroso natural products.

A General Procedure for Synthesis of NG-Alkyl, and NG-Aryl-L-Arginines as Potential Nitric Oxide Synthase Inhibitors

A general procedure for the synthesis of NG-alkyl, and NG-aryl-L-arginines with relatively high overall yield is reported. The key step involved the coupling of protected L-ornithine 4 with isothiourea 7 to give the fully protected NG-aryl-L-arginine derivative 8. Subsequent deprotection of 8 in acidic condition provided the final target compound 9 with an overall yield of more than 80%.

A facile route to cyclic and acyclic alkyl-arginines

Treatment of commercially available alkyl and cycloalkyl thioureas with methyl iodide provides the corresponding S-alkylisothiouronium iodide which reacts directly with ornithine to yield the title compounds.

A highly efficient preparation of N(G)-methyl-L-arginine and N(G)-methyl-D-arginine

A convenient procedure for the preparation and purification of N(G)-methyl-L-arginine and N(G)-methyl-D-arginine acetate salts is described.

Multigram synthesis of N(G)-methyl-(L)-arginine and its analytical characterization

A multigram preparation and analytical characterization of N(G)-methyl-(L)-arginine (L-NMMA) 1, the most important inhibitor of the biosynthesis of Endothelium-Derived Relaxing Factor (EDRF), is reported.