Cyclo(His-Pro) forms a diketopiperazine ring uniting histidine and proline in a compact cyclic scaffold. The imidazole side chain contributes metal-binding and acid-base properties, while proline enforces conformational rigidity. Researchers use it as a model for endogenous cyclic dipeptides and neuromodulatory motifs. Applications span food chemistry, neurobiochemistry, and cyclic-peptide structure studies.
CAT No: R2707
CAS No:53109-32-3
Synonyms/Alias:Cyclo(his-pro);Cyclo(-His-Pro);53109-32-3;Cyclo(L-His-L-Pro);UNII-Q10817UXVT;Q10817UXVT;L-His-L-Pro-DKP;L,L-cyclo(histidylprolyl);Cyclo(L-histidyl-L-proline);MLS000028694;CHEBI:90039;CYCLO-(L-HISTIDINE-L-PROLINE) INHIBITOR;SMR000058881;(3S,8aS)-3-(1H-Imidazol-4-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;(3S,8aS)-3-[(1H-imidazol-5-yl)methyl]hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;(3S,8AS)-3-(1H-IMIDAZOL-5-YLMETHYL)-2,3,6,7,8,8A-HEXAHYDROPYRROLO(1,2-A)PYRAZINE-1,4-DIONE;(3S,8aS)-3-((1H-imidazol-5-yl)methyl)-octahydropyrrolo(1,2-a)pyrazine-1,4-dione;(3S,8aS)-3-((1H-imidazol-5-yl)methyl)hexahydropyrrolo(1,2-a)pyrazine-1,4-dione;(3S,8aS)-3-(1H-Imidazol-4-ylmethyl)hexahydropyrrolo(1,2-a)pyrazine-1,4-dione;(3S,8aS)-3-[(1H-imidazol-5-yl)methyl]-octahydropyrrolo[1,2-a]pyrazine-1,4-dione;MFCD00133207;1w1t;Opera_ID_1205;Cyclo(histidyl-proline);Histidylproline diketopiperazine;cyclo[l-histidyl-l-prolyl];CHEMBL188225;SCHEMBL2039884;SCHEMBL12228287;DTXSID90962567;(3S,8aS)-3-((1H-imidazol-4-yl)methyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;HMS2234D12;CS-6320;DB02414;FC49257;(3S,8AR)-3-(1H-IMIDAZOL-5-YLMETHYL)HEXAHYDROPYRROLO[1,2-A]PYRAZINE-1,4-DIONE;HY-101402;NS00069934;G85416;Q27286866;(3S,8aS)-3-(1H-imidazol-5-ylmethyl)hexahydropyrrolo[1,2-a]pyrazine-1,4-dione;
Cyclo(his-pro), also known as cyclic L-histidyl-L-proline or CHP, is a naturally occurring cyclic dipeptide composed of the amino acids histidine and proline. Its unique cyclic structure imparts notable stability and distinct biochemical properties, making it an intriguing subject in peptide chemistry and molecular biology. As an endogenous diketopiperazine, cyclo(his-pro) is found in various biological systems, where it is implicated in multiple physiological processes. The compound's resistance to enzymatic degradation, coupled with its ability to interact with diverse cellular targets, underpins its growing significance in research focused on peptide signaling, neurochemistry, and metabolic regulation.
Peptide signaling studies: Cyclo(his-pro) serves as a valuable tool for investigating peptide-mediated signaling pathways. Its endogenous presence in mammalian tissues, particularly in neural and endocrine systems, has prompted extensive research into its role as a neuromodulator and signaling molecule. Researchers utilize CHP to elucidate the mechanisms underlying peptide transport, receptor activation, and downstream signaling cascades, thereby contributing to a deeper understanding of cellular communication and regulatory networks.
Neurochemical research: The compound is frequently employed in neurochemical studies exploring neurotransmitter modulation and synaptic function. Due to its structural similarity to certain neuropeptides, CHP is used to examine its influence on neurotransmitter release, uptake, and metabolism. Experimental models leverage its stability and bioactivity to dissect the complex interplay between peptide modulators and classical neurotransmitter systems, advancing knowledge in neurobiology and cognitive science.
Metabolic pathway analysis: Cyclo(his-pro) is instrumental in studies of amino acid metabolism and cyclic dipeptide biosynthesis. Its formation from precursor amino acids provides a model for understanding enzymatic cyclization reactions and the regulation of diketopiperazine production. By tracking the synthesis and catabolism of CHP in vitro and in vivo, researchers gain insights into metabolic flux, enzyme specificity, and the physiological roles of small cyclic peptides in health and disease.
Analytical method development: The distinctive physicochemical properties of CHP make it a useful standard and reference compound in analytical chemistry. It is routinely employed in the development and validation of chromatographic and spectrometric techniques designed to detect and quantify cyclic dipeptides in complex biological samples. The availability of highly characterized CHP facilitates the optimization of sample preparation protocols, method calibration, and the assessment of analytical specificity and sensitivity.
Peptide stability and structure-function studies: Cyclo(his-pro) is commonly utilized in research focused on peptide stability, conformational analysis, and structure-activity relationships. Its resistance to proteolytic cleavage and defined cyclic conformation provide a robust model for evaluating the impact of cyclization on peptide properties. Investigations employing CHP contribute to the rational design of stable peptide analogs and the development of novel bioactive molecules with enhanced pharmacokinetic profiles for research applications.
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