Carnosine, D-

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.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Carnosine, D-(CAS 5853-00-9)

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;

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M.F/Formula
C9H14N4O3
M.W/Mr.
226.23
Sequence
One Letter Code:XH
Three Letter Code:H-bAla-D-His-OH

Carnosine, D-, a dipeptide composed of D-beta-alanine and L-histidine, is a synthetic analog of the naturally occurring carnosine found in various tissues. Distinguished by the D-configuration of its beta-alanine residue, this compound exhibits unique physicochemical properties and enhanced resistance to enzymatic degradation compared to its L-form counterpart. Carnosine, D- is highly valued in biochemical research and experimental biology due to its stability and potential for modulating cellular processes. Its ability to interact with metal ions, scavenge reactive species, and influence protein glycation pathways makes it a versatile tool for a range of scientific investigations. The compound's synthetic accessibility and well-defined structure further support its integration into advanced laboratory protocols, enabling researchers to explore its multifaceted roles in vitro and in vivo systems.

Antioxidant Mechanism Studies: In the context of oxidative stress research, Carnosine, D- serves as an effective model for elucidating non-enzymatic antioxidant mechanisms. Its robust ability to neutralize reactive oxygen and nitrogen species, coupled with its resistance to carnosinase-mediated hydrolysis, allows for prolonged observation of its protective effects in cell cultures and tissue extracts. Researchers employ D-carnosine to dissect the pathways by which dipeptides mitigate oxidative damage, providing insights into the stabilization of cellular components under stress conditions. The compound's interactions with lipid peroxidation products and free radicals are particularly relevant for developing antioxidant strategies in experimental systems.

Metal Chelation Research: D-carnosine's strong affinity for transition metal ions such as copper and zinc underpins its application in metal chelation studies. By forming stable complexes with these ions, it enables the investigation of metal-induced cytotoxicity and the modulation of metal-dependent enzymatic reactions. Scientists utilize D-carnosine to probe the molecular basis of metal homeostasis, assess the prevention of metal-catalyzed oxidative reactions, and explore potential interventions for metal overload in cellular models. The stereochemical configuration of D-carnosine offers distinct binding characteristics, making it a valuable probe for differentiating the effects of dipeptide isomers in chelation assays.

Glycation Inhibition Assays: The utility of Carnosine, D- in glycation research stems from its ability to inhibit the formation of advanced glycation end-products (AGEs) in protein-sugar model systems. By interfering with the Maillard reaction, D-carnosine helps elucidate the mechanisms that underlie protein modification and aggregation under hyperglycemic conditions. Researchers leverage its stability to perform long-term assays, monitoring the suppression of AGEs formation and evaluating the protective effects on protein function and structure. These studies contribute to a deeper understanding of glycation-related cellular dysfunction and the development of anti-glycation strategies.

Protein and Peptide Modification Studies: D-carnosine is frequently employed to investigate the modification of proteins and peptides under various stressors. Its reactivity with carbonyl compounds and aldehydes allows for the assessment of protein cross-linking and aggregation pathways. Through incubation with target proteins, D-carnosine facilitates the identification of modification sites and the characterization of structural changes, supporting research into protein aging, misfolding, and degradation. The compound's unique stereochemistry provides an additional dimension for studying the influence of peptide configuration on modification kinetics and outcomes.

Cellular Stress Response Modeling: The application of Carnosine, D- extends to modeling cellular responses to environmental and metabolic stress. In cultured cells and tissue models, it is used to simulate protective mechanisms against oxidative, glycation, and metal-induced insults. By incorporating D-carnosine into experimental protocols, researchers can monitor changes in gene expression, enzyme activity, and cellular viability, thereby dissecting the pathways involved in stress adaptation. This approach aids in the identification of molecular targets and the development of novel strategies to enhance cellular resilience in challenging environments.

In summary, Carnosine, D- offers a robust platform for advancing scientific understanding across multiple domains, including antioxidant defense, metal chelation, glycation inhibition, protein modification, and cellular stress response. Its unique structural and functional attributes provide researchers with a versatile tool for probing complex biochemical processes and developing innovative experimental approaches.

InChI
InChI=1S/C9H14N4O3/c10-2-1-8(14)13-7(9(15)16)3-6-4-11-5-12-6/h4-5,7H,1-3,10H2,(H,11,12)(H,13,14)(H,15,16)/t7-/m1/s1
InChI Key
CQOVPNPJLQNMDC-SSDOTTSWSA-N

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