alpha-Casozepine is a fragment of alpha(s1)-casein with anxiolytic activity.
CAT No: R1908
CAS No:117592-45-7
Synonyms/Alias:alpha-Casozepine;lactium;117592-45-7;I24KIH8EZS;UNII-I24KIH8EZS;ZYLKENE;.ALPHA.-CASOZEPINE;ALPHA-CASOZEPINE [WHO-DD];TYR-LEU-GLY-TYR-LEU-GLU-GLN-LEU-LEU-ARG;(2S,5S,8S,11S,14S)-11-(3-amino-3-oxopropyl)-14-((2S,5S,11S,14S)-14-amino-5-(4-hydroxybenzyl)-15-(4-hydroxyphenyl)-2,11-diisobutyl-4,7,10,13-tetraoxo-3,6,9,12-tetraazapentadecanamido)-2-(3-guanidinopropyl)-5,8-diisobutyl-4,7,10,13-tetraoxo-3,6,9,12-tetraazaheptadecanedioic acid;L-ARGININE, L-TYROSYL-L-LEUCYLGLYCYL-L-TYROSYL-L-LEUCYL-L-.ALPHA.-GLUTAMYL-L-GLUTAMINYL-L-LEUCYL-L-LEUCYL-;L-TYROSYL-L-LEUCYLGLYCYL-L-TYROSYL-L-LEUCYL-L-.ALPHA.-GLUTAMYL-L-GLUTAMINYL-L-LEUCYL-L-LEUCYL-L-ARGININE;|A-Casozepine;SCHEMBL22413050;HY-P2602;AKOS040750345;L-ARGININE, L-TYROSYL-L-LEUCYLGLYCYL-L-TYROSYL-L-LEUCYL-L-ALPHA-GLUTAMYL-L-GLUTAMINYL-L-LEUCYL-L-LEUCYL-;L-TYROSYL-L-LEUCYLGLYCYL-L-TYROSYL-L-LEUCYL-L-ALPHA-GLUTAMYL-L-GLUTAMINYL-L-LEUCYL-L-LEUCYL-L-ARGININE;
Chemical Name:(4S)-5-[[(2S)-5-amino-1-[[(2S)-1-[[(2S)-1-[[(1S)-1-carboxy-4-(diaminomethylideneamino)butyl]amino]-4-methyl-1-oxopentan-2-yl]amino]-4-methyl-1-oxopentan-2-yl]amino]-1,5-dioxopentan-2-yl]amino]-4-[[(2S)-2-[[(2S)-2-[[2-[[(2S)-2-[[(2S)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]acetyl]amino]-3-(4-hydroxyphenyl)propanoyl]amino]-4-methylpentanoyl]amino]-5-oxopentanoic acid
Alpha-Casozepine is a bioactive peptide derived from the enzymatic hydrolysis of bovine casein, specifically from the αs1-casein fraction. As a naturally occurring peptide, it has garnered significant attention within the biochemical research community due to its unique sequence and functional properties. Its structure enables it to interact with various molecular targets, making it a valuable tool for investigating peptide-receptor interactions, neurochemical pathways, and the broader physiological roles of dietary peptides. Alpha-Casozepine serves as a model compound in studies exploring the relationship between dietary proteins, peptide bioavailability, and biological signaling mechanisms, offering researchers a robust platform for advancing knowledge in peptide biochemistry and functional food science.
Peptide-receptor interaction studies: Alpha-Casozepine is widely employed in research focused on the characterization of peptide-receptor interactions, particularly those involving neurotransmitter systems in the central nervous system. Its affinity for certain receptor subtypes allows for the elucidation of peptide binding mechanisms, receptor specificity, and downstream signaling events. By using this peptide, scientists can dissect the structural requirements for receptor activation or inhibition, contributing to a deeper understanding of how dietary peptides modulate neurochemical pathways at a molecular level.
Functional food and nutraceutical research: The peptide's origin from milk proteins makes it an important candidate for studies investigating the health-promoting properties of dairy-derived bioactive components. Researchers utilize alpha-Casozepine to assess its functional impact on various physiological systems, including stress response and mood regulation, within the context of functional food development. Its incorporation into model food systems enables the evaluation of peptide stability, bioavailability, and efficacy, supporting the formulation of nutraceutical products with scientifically validated benefits.
Peptide structure-activity relationship (SAR) analysis: Alpha-Casozepine provides a well-defined sequence for structure-activity relationship studies, which are essential for mapping the critical residues responsible for its biological effects. Through systematic modification and analysis, researchers can identify the structural motifs that confer receptor affinity, stability, or resistance to enzymatic degradation. These insights inform the rational design of novel peptides with tailored properties for use in both basic research and applied biotechnology.
Enzymatic hydrolysis process optimization: As a model substrate, alpha-Casozepine is utilized in the optimization of enzymatic hydrolysis protocols aimed at generating bioactive peptides from dairy proteins. Its predictable generation and measurable activity allow process engineers and food scientists to fine-tune enzymatic conditions, assess yield and purity, and develop scalable methods for peptide production. This application is particularly relevant for the dairy industry and for research groups focused on sustainable production of high-value functional ingredients.
Analytical method development: The unique sequence and physicochemical characteristics of alpha-Casozepine make it a valuable standard for developing and validating analytical techniques such as high-performance liquid chromatography (HPLC), mass spectrometry, and capillary electrophoresis. Its use as a reference peptide facilitates the accurate identification, quantification, and characterization of similar bioactive peptides in complex biological or food matrices. This supports quality control, regulatory compliance, and advanced research into peptide profiles in both academic and industrial settings.
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