H-Ile-Pro-Pro-OH, a milk-derived peptide, inhibits angiotensin-converting enzyme (ACE) with an IC50 of 5 μM. Antihypertensive tripeptides.
CAT No: 10-101-251
CAS No:26001-32-1
Synonyms/Alias:H-ILE-PRO-PRO-OH;26001-32-1;isoleucyl-prolyl-proline;l-isoleucyl-l-prolyl-l-proline;CHEMBL190994;(2S)-1-[(2S)-1-[(2S,3S)-2-AMINO-3-METHYLPENTANOYL]PYRROLIDINE-2-CARBONYL]PYRROLIDINE-2-CARBOXYLIC ACID;isoleucine-proline-proline;L-Proline, L-isoleucyl-L-prolyl-;MFCD08458621;SCHEMBL1646849;L-Proline,L-isoleucyl-L-prolyl-;CHEBI:158716;BDBM50169149;DA-53997;HY-114424;CS-0085280;(S)-1-((S)-1-((2S,3S)-2-Amino-3-methylpentanoyl)pyrrolidine-2-carbonyl)pyrrolidine-2-carboxylic acid;(S)-1-[(S)-1-((2S,3S)-2-Amino-3-methyl-pentanoyl)-pyrrolidine-2-carbonyl]-pyrrolidine-2-carboxylic acid;
Ile-Pro-Pro, also known as isoleucyl-prolyl-proline, is a tripeptide composed of the amino acids isoleucine, proline, and proline in sequence. As a bioactive peptide derived primarily from the enzymatic hydrolysis of food proteins such as casein, it has garnered significant attention in scientific research due to its unique structural characteristics and physiological relevance. The presence of two consecutive proline residues imparts notable resistance to enzymatic degradation, enhancing its stability in various biological and food systems. Researchers value this tripeptide for its ability to interact with specific peptide receptors and enzymes, making it a promising molecule for both in vitro and in vivo studies. Its versatility and bioactivity have established it as a valuable tool in diverse research fields, ranging from biochemistry and molecular biology to food science and nutraceutical development.
Peptide-based functional food research: Ile-Pro-Pro is widely utilized in the development and evaluation of functional foods, particularly those aimed at supporting cardiovascular health and metabolic balance. Its integration into food matrices allows scientists to investigate the peptide's stability during food processing and digestion, as well as its potential for bioavailability and bioactivity after oral administration. Studies often focus on incorporating this tripeptide into dairy products, beverages, and supplements, examining its interactions with other food components and its capacity to deliver targeted physiological benefits through diet.
Biochemical mechanism studies: In the realm of biochemical research, isoleucyl-prolyl-proline serves as a model compound for exploring peptide-enzyme interactions and receptor binding dynamics. Its unique sequence, especially the double proline motif, is instrumental in elucidating the specificity of peptidases and the structural requirements for peptide recognition by biological targets. Researchers utilize synthetic and labeled versions of this tripeptide to probe enzymatic cleavage patterns, map active sites, and understand the molecular mechanisms underpinning peptide-mediated signaling pathways.
Nutraceutical ingredient innovation: As a naturally occurring peptide with demonstrated bioactivity, Ile-Pro-Pro is a focal point in the innovation of nutraceutical ingredients. Scientists and product developers explore its incorporation into dietary supplements aimed at promoting general wellness. Research efforts often assess the peptide's compatibility with various excipients, its stability during storage, and its potential synergistic effects when combined with other bioactive compounds. These investigations help pave the way for the creation of novel nutraceutical formulations that harness the inherent properties of bioactive peptides.
In vitro cell culture studies: The tripeptide is frequently employed in in vitro experiments to evaluate its effects on cellular functions and gene expression. By treating cultured cell lines with isoleucyl-prolyl-proline, researchers can monitor changes in cellular signaling pathways, oxidative stress responses, and other physiological processes. These studies provide valuable insights into the cellular mechanisms influenced by bioactive peptides and contribute to the broader understanding of peptide-based modulation of biological systems.
Peptide stability and delivery system research: Ile-Pro-Pro's resistance to proteolytic degradation makes it an ideal candidate for studies focused on peptide delivery systems and stability enhancement. Scientists investigate encapsulation techniques, such as liposomes or nanoparticles, to protect the peptide during gastrointestinal transit and optimize its release profile. These efforts aim to improve the oral bioavailability and targeted delivery of bioactive peptides, supporting the development of advanced functional foods and supplement products.
Overall, the application landscape for Ile-Pro-Pro continues to expand as research uncovers new facets of its biological activity and technological potential. Its role in functional food development, biochemical mechanism studies, nutraceutical innovation, in vitro cellular research, and delivery system optimization underscores its significance as a multifaceted tool in the scientific and industrial communities.
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