[Leu³]-Oxytocin

H-Cys(1)-DL-Tyr-Leu-DL-Gln-Asn-DL-Cys(1)-Pro-Leu-Gly-NH2 is a synthetic carbohydrate-derived peptide sequence notable for its unique arrangement of amino acid residues and the presence of both L- and DL-forms. This compound is designed to facilitate advanced biochemical research, offering a versatile platform for studies involving peptide interactions, structure-activity relationships, and molecular recognition. The sequence incorporates cysteine residues at strategic positions, which allow for the formation of disulfide bridges and contribute to the stability and conformational diversity of the molecule. The presence of glycine at the C-terminal end, capped with an amide group, further enhances its utility in mimicking naturally occurring peptide backbones and in supporting various research applications that require stable, bioactive conformations.

Peptide Structure-Activity Relationship Studies: H-Cys(1)-DL-Tyr-Leu-DL-Gln-Asn-DL-Cys(1)-Pro-Leu-Gly-NH2 is extensively employed in structure-activity relationship (SAR) investigations, where researchers analyze how specific modifications in the peptide sequence affect its biological or biochemical properties. By systematically substituting L- and DL-amino acids, scientists can elucidate the role of stereochemistry in molecular recognition, binding affinity, and functional activity. This enables the rational design of peptides with tailored properties for use in various experimental models and enhances the understanding of how peptide structure influences function at the molecular level.

Protein-Protein Interaction Analysis: The unique sequence of this peptide makes it an excellent tool for studying protein-protein interactions. Researchers utilize it as a probe or ligand to investigate binding sites, interaction partners, and conformational changes in target proteins. The presence of cysteine residues allows for site-specific labeling or cross-linking, which aids in mapping interaction interfaces and identifying critical contact points. Such studies are vital for deciphering complex signaling pathways and for the development of new molecular tools to modulate protein function in vitro.

Enzyme Substrate and Inhibitor Research: H-Cys(1)-DL-Tyr-Leu-DL-Gln-Asn-DL-Cys(1)-Pro-Leu-Gly-NH2 serves as a model substrate or inhibitor in enzymology research, particularly for enzymes that recognize or modify peptide substrates. The inclusion of both L- and DL-amino acids provides a means to test enzyme specificity, substrate preferences, and catalytic mechanisms. By observing how enzymes process or interact with this peptide, researchers can identify key determinants of enzymatic activity and develop more selective inhibitors for use in biochemical assays.

Molecular Recognition and Binding Assays: The peptide is widely used in molecular recognition studies, where its sequence diversity and structural features enable the exploration of binding affinities with various biomolecules, such as antibodies, receptors, or nucleic acids. By immobilizing or labeling the peptide, scientists can perform binding assays to quantify interactions, assess selectivity, and screen for novel binding partners. These experiments contribute to the development of diagnostic tools, biosensors, and affinity reagents for research and analytical applications.

Biomaterials and Surface Modification: H-Cys(1)-DL-Tyr-Leu-DL-Gln-Asn-DL-Cys(1)-Pro-Leu-Gly-NH2 is also applied in the field of biomaterials, where its cysteine residues facilitate covalent attachment to gold or other metal surfaces via thiol chemistry. This property is exploited to create functionalized surfaces for cell culture, biosensing, or tissue engineering applications. The peptide's ability to promote specific cell adhesion or to present bioactive motifs on material surfaces supports the design of advanced biomaterials with tailored biological interactions.

Peptide Conformation and Folding Studies: Researchers leverage this peptide to investigate the principles governing peptide folding, disulfide bond formation, and conformational stability. By analyzing the structural transitions and folding pathways of the sequence, insights can be gained into the determinants of peptide stability, the role of specific residues in folding kinetics, and the formation of secondary structures. Such studies are instrumental in advancing the understanding of peptide chemistry and in informing the design of novel bioactive molecules for diverse scientific applications.

1. C-peptide and its C-terminal fragments improve erythrocyte deformability in type 1 diabetes patients

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4. Store-operated Ca2+ entry sustains the fertilization Ca2+ signal in pig eggs

5. Identification, Localization in the Central Nervous System and Novel Myostimulatory Effect of Allatostatins in Tenebrio molitor Beetle