H-Gly-D-Tyr-OH incorporates a D-tyrosine residue that perturbs typical backbone geometry and hydrogen-bond patterns. Researchers use it to evaluate stereochemical influences on folding and recognition. Its aromatic side chain supports UV-based analytical work. Applications span chirality studies, peptide-design research, and structure-function mapping.
CAT No: R2554
CAS No:133706-65-7
Synonyms/Alias:H-Gly-D-Tyr-OH;133706-65-7;D-Tyrosine, N-glycyl-;(2R)-2-(2-AMINOACETAMIDO)-3-(4-HYDROXYPHENYL)PROPANOIC ACID;MFCD02259554;SCHEMBL3459805;(2R)-2-[(2-aminoacetyl)amino]-3-(4-hydroxyphenyl)propanoic acid;DA-64148;FG108317;HY-131094;CS-0128295;EN300-7442707;
H-Gly-D-Tyr-OH, also known as Glycyl-D-tyrosine, is a synthetic dipeptide composed of glycine and the D-enantiomer of tyrosine. As a member of the peptide compound class, it serves as a versatile research tool in biochemistry and molecular biology. The incorporation of a D-amino acid residue imparts unique physicochemical properties, including enhanced resistance to proteolytic degradation and altered conformational behavior compared to its L-counterpart. These attributes make Glycyl-D-tyrosine valuable for probing peptide stability, investigating stereochemical effects in peptide function, and modeling non-natural peptide structures. Its defined sequence and chirality position it as a key reagent for advancing the understanding of peptide-based systems and for supporting a range of experimental applications in academic and industrial research settings.
Peptide stability studies: Glycyl-D-tyrosine is frequently employed in studies designed to assess the impact of D-amino acid incorporation on peptide backbone stability and resistance to enzymatic hydrolysis. The presence of the D-tyrosine residue makes the dipeptide less susceptible to degradation by common proteases, thereby enabling researchers to systematically compare the stability profiles of D-containing versus all-L analogs. These investigations are crucial for developing peptide-based biomaterials, drug delivery systems, and enzyme-resistant peptide probes.
Stereochemical analysis: The dipeptide is a valuable model system for elucidating the effects of stereochemistry on peptide structure and function. By examining the conformational preferences and intermolecular interactions of Glycyl-D-tyrosine, researchers can gain insights into how D-amino acid residues influence peptide folding, aggregation, and recognition events. Such studies contribute to the broader understanding of chiral discrimination in biological systems and inform the rational design of novel peptides with tailored properties.
Peptide synthesis validation: In the context of solid-phase peptide synthesis (SPPS) and related methodologies, Glycyl-D-tyrosine is used as a reference compound or intermediate to validate synthetic protocols involving D-amino acids. Its defined sequence and straightforward analytical profile make it suitable for calibrating chromatographic and spectrometric techniques, optimizing coupling conditions, and verifying enantiomeric purity in synthetic workflows. This ensures the reliability and reproducibility of peptide synthesis processes, which is essential for both research and industrial peptide production.
Biochemical assay development: The unique structural features of this dipeptide allow it to serve as a substrate or control in the development of biochemical assays targeting peptidases, transporters, or binding proteins with specificity for D-amino acid-containing sequences. By incorporating Glycyl-D-tyrosine into assay platforms, scientists can evaluate the selectivity and activity of enzymes or receptors, facilitating the characterization of novel biochemical pathways and the screening of modulatory compounds.
Functional peptide design: Researchers leverage the properties of Glycyl-D-tyrosine in the design and testing of functional peptides with enhanced stability or altered biological activity. The strategic placement of D-tyrosine within peptide sequences can modulate receptor binding, influence self-assembly, or confer resistance to metabolic breakdown, depending on the intended application. As such, this dipeptide serves as a foundational building block for the exploration of non-natural peptide architectures and the development of advanced peptide-based materials.
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