Carnosine, D- is a dipeptide analog featuring β-alanine linked to D-histidine, creating a stereochemically distinct backbone. Researchers employ it to examine imidazole-driven interactions, metal coordination, and redox behavior. The motif supports studies of proton buffering and conformational variability.
CAT No: R2328
CAS No:5853-00-9
Synonyms/Alias:Carnosine, D-;5853-00-9;d-carnosine;beta-alanyl-d-histidine;LE2264A962;(2R)-2-(3-aminopropanoylamino)-3-(1H-imidazol-5-yl)propanoic acid;(2R)-2-(3-aminopropanamido)-3-(1H-imidazol-5-yl)propanoic acid;UNII-LE2264A962;D-Histidine, N-.beta.-alanyl-;D-Histidine, b-alanyl-;D-Histidine, N-beta-alanyl-;CARNOSINE D-FORM [MI];SCHEMBL1161010;(3-Aminopropanoyl)-D-histidine;SCHEMBL22392772;DTXSID201319103;D-HISTIDINE, .BETA.-ALANYL-;NCGC00095651-01;FC184107;Q27282939;Z1543388927;
Carnosine, D- is a synthetic dipeptide composed of D-β-alanine and L-histidine, representing the enantiomeric form of the naturally occurring L-carnosine. As a non-proteinogenic peptide, it is structurally similar to its L-counterpart but exhibits distinct biochemical properties due to the D-configuration of the β-alanine residue. This stereochemical modification imparts unique resistance to enzymatic degradation by carnosinases, making D-carnosine a valuable tool for investigating peptide metabolism, stability, and function in various biological and chemical systems. Its capacity to participate in metal ion chelation, antioxidant studies, and protein interaction assays has established its relevance in advanced peptide research and analytical biochemistry.
Peptide stability research: D-carnosine is frequently employed as a model compound to explore the impact of stereochemistry on peptide stability in biological environments. The substitution of D-β-alanine confers pronounced resistance to enzymatic hydrolysis, particularly by carnosinase enzymes that readily degrade the natural L-form. This property allows researchers to delineate the metabolic fate of dipeptides, differentiate between enzymatic and non-enzymatic degradation pathways, and assess the influence of peptide backbone configuration on bioavailability and persistence in vitro and in vivo.
Enzyme specificity assays: The use of D-carnosine in enzyme specificity studies provides critical insights into the substrate selectivity of peptidases and dipeptidases. By comparing the hydrolysis rates of D- and L-forms, investigators can characterize the stereochemical preferences of various proteolytic enzymes. Such assays are instrumental in elucidating the mechanisms underlying peptide recognition, guiding the design of enzyme inhibitors, and advancing the development of stable peptide-based biomolecules for research applications.
Metal ion chelation studies: Owing to its imidazole-containing histidine residue, D-carnosine serves as an effective ligand in metal ion binding experiments. Its resistance to enzymatic breakdown enables prolonged investigation of metal-peptide interactions under physiological and non-physiological conditions. Researchers utilize D-carnosine to probe the coordination chemistry of transition metals, evaluate the effects of peptide stereochemistry on chelation efficacy, and model the role of dipeptides in metal homeostasis and detoxification processes.
Antioxidant mechanism analysis: D-carnosine is also utilized in the examination of antioxidant mechanisms at the molecular level. Its structural similarity to L-carnosine, combined with enhanced stability, makes it an ideal reference compound for dissecting the radical scavenging properties of dipeptides. Studies often focus on comparing the ability of D- and L-forms to quench reactive oxygen species, inhibit lipid peroxidation, and mitigate oxidative damage in controlled biochemical assays, thereby advancing understanding of structure-activity relationships in peptide antioxidants.
Peptide transport and uptake investigations: The unique configuration of D-carnosine renders it a valuable probe for studying peptide transport systems, including oligopeptide transporters in cellular and subcellular models. Its altered recognition by peptide transporters, compared to the L-form, allows for the dissection of stereospecificity in uptake mechanisms. Experimental use of D-carnosine supports the identification of transport pathways, informs the design of peptide-based delivery vehicles, and aids in the development of strategies to modulate peptide absorption in research settings.
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