783265-75-8

Basic information

• Product Name: N-w,w-diMethy-D-arginine(asyMMetrical)
• Synonyms: N-w,w-diMethy-D-arginine(asyMMetrical);D-Arg(Me, Me)-OH (asyMMetrical);(R)-2-Amino-5-((bis(methylamino)methylene)amino)pentanoic acid;D-ARG(ME,ME)-OH
• CAS NO: 783265-75-8
• Molecular Formula: C8H18N4O2
• Molecular Weight: 202.25412
• Mol File: 783265-75-8.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• Storage Temp.: Sealed in dry,Room Temperature
• CAS DataBase Reference: N-w,w-diMethy-D-arginine(asyMMetrical)(CAS DataBase Reference)
• NIST Chemistry Reference: N-w,w-diMethy-D-arginine(asyMMetrical)(783265-75-8)
• EPA Substance Registry System: N-w,w-diMethy-D-arginine(asyMMetrical)(783265-75-8)

Safety Data

• Hazardous Substances Data: 783265-75-8(Hazardous Substances Data)

Usage

General Description

Nω,Nω-Dimethyl-L-arginine (asymmetrical) is a chemical compound that acts as a competitive inhibitor of nitric oxide synthase, leading to a decrease in the production of nitric oxide. It is a methylated form of the amino acid arginine and is known to be involved in the regulation of cardiovascular function and blood pressure. Elevated levels of Nω,Nω-dimethyl-L-arginine have been linked to various cardiovascular diseases, such as hypertension and atherosclerosis. It is also considered to be a potential biomarker for the assessment of endothelial dysfunction. N-w,w-Dimethy-D-arginine(asymmetrical) is of interest in the field of research on nitric oxide regulation and its implications for cardiovascular health.

Relevant articles and documents

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.