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 bioactive tripeptide composed of the amino acids isoleucine, proline, and proline. As a member of the peptide compound class, it is of significant interest in biochemical and physiological research due to its structural features and functional properties. The presence of two consecutive proline residues imparts conformational rigidity, influencing its interaction with biological targets and enzymatic stability. Researchers value this tripeptide for its potential roles in modulating enzymatic pathways, studying peptide transport and metabolism, and exploring structure-activity relationships within the broader context of peptide science.
Peptide bioactivity studies: Ile-Pro-Pro is frequently employed in investigations of peptide-mediated bioactivity, particularly in relation to its capacity to modulate specific enzymatic processes. Its unique sequence allows researchers to probe the effects of proline-rich motifs on enzyme recognition, binding affinity, and resistance to proteolytic degradation. Such studies help elucidate the mechanisms by which short peptides can influence biological systems, providing foundational knowledge for peptide pharmacology and functional food research.
Enzymatic substrate specificity: The tripeptide serves as a model substrate for examining the specificity and kinetics of various peptidases, including prolyl endopeptidases and dipeptidyl peptidases. By utilizing Ile-Pro-Pro in enzymatic assays, scientists can characterize the cleavage preferences of these enzymes, assess their activity under different conditions, and investigate the impact of sequence modifications on substrate turnover. These insights are valuable for understanding proteolytic processing in physiological and industrial contexts.
Peptide transport and absorption: Due to its structural properties, Ile-Pro-Pro is utilized in studies of peptide transport across biological membranes, such as those mediated by peptide transporters in the intestinal epithelium. Its resistance to rapid degradation makes it a suitable candidate for tracing absorption pathways, evaluating transporter specificity, and modeling the bioavailability of dietary peptides. This application supports research into nutrient absorption, peptide-based delivery systems, and the design of functional ingredients.
Structure-activity relationship (SAR) analysis: Researchers employ this tripeptide to investigate how specific amino acid sequences and conformational constraints influence biological activity. The presence of two proline residues in succession offers a platform for dissecting the relationship between peptide structure and function, informing the rational design of bioactive peptides with tailored properties. SAR studies using Ile-Pro-Pro contribute to advances in peptide engineering, biomaterials development, and the optimization of peptide-based research tools.
Peptide synthesis benchmarking: In the context of synthetic peptide chemistry, Ile-Pro-Pro is used as a reference sequence for evaluating coupling efficiency, protecting group strategies, and purification protocols. Its moderate length and challenging proline-proline junction provide a practical test case for optimizing solid-phase peptide synthesis workflows. Results obtained with this tripeptide can guide the development of robust synthetic methodologies, supporting both research-scale and industrial peptide production.
2. Cell-based adhesion assays for isolation of snake venom’s integrin antagonists
4. Immune responses to homocitrulline-and citrulline-containing peptides in rheumatoid arthritis
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