Lonodelestat is a peptide analog constructed from aromatic, hydrophobic, and polar residues arranged to promote structured folding and surface interactions. Researchers use it to examine ligand-protein binding, secondary-structure transitions, and conformational energetics. Its balanced composition suits advanced biophysical analysis.
CAT No: R2420
CAS No:906547-89-5
Synonyms/Alias:Lonodelestat;Lonodelestat [INN];5SD2VOV3MF;906547-89-5;UNII-5SD2VOV3MF;POL6014;1,13-Anhydro(L-alanyl-L-seryl-L-isoleucyl-L-prolyl-lprolyl-L-glutaminyl-L-lysyl-L-tyrosyl-D-prolyl-L-prolyl-(2S)-2-aminodecanoyl-L-alpha-glutamyl-L-threonine);Cyclo(L-alanyl-L-seryl-L-isoleucyl-L-prolyl-L-prolyl-L-glutaminyl-L-lysyl-L-tyrosyl-D-prolyl-L-prolyl-(2S)-2-aminodecanoyl-L-alpha-glutamyl-L-threonyl);cyclo[Ala-Ser-Ile-Pro-Pro-Gln-Lys-Tyr-D-Pro-Pro-Nle(Bu)-Glu-Thr];1,13-ANHYDRO(L-ALANYL-L-SERYL-L-ISOLEUCYL-L-PROLYL-LPROLYL-L-GLUTAMINYL-L-LYSYL-L-TYROSYL-D-PROLYL-L-PROLYL-(2S)-2-AMINODECANOYL-L-.ALPHA.-GLUTAMYL-L-THREONINE);CYCLO(L-ALANYL-L-SERYL-L-ISOLEUCYL-L-PROLYL-L-PROLYL-L-GLUTAMINYL-L-LYSYL-L-TYROSYL-D-PROLYL-L-PROLYL-(2S)-2-AMINODECANOYL-L-.ALPHA.-GLUTAMYL-L-THREONYL);cyclo(Ala-Ser-Ile-Pro-Pro-Gln-Lys-Tyr-D-Pro-Pro-Nle(Bu)-Glu-Thr);GTPL11275;HY-P3293;POL-6014;AKOS040758444;DA-65052;CS-0204184;Cyclo[L-alanyl-L-seryl-L-isoleucyl-L-prolyl-L-prolyl-L-glutaminyl-L-lysyl-L-tyrosyl-D-prolyl-L-prolyl-(2S)-2-aminodecanoyl-L-alpha-glutamyl-L-threonyl] (9CI);
Lonodelestat is a synthetic peptide inhibitor designed to target and modulate the enzymatic activity of human neutrophil elastase (HNE), a serine protease implicated in the regulation of inflammatory processes and tissue remodeling. As a highly specific peptide-based compound, lonodelestat serves as a valuable tool for dissecting protease-driven pathways in cellular and molecular biology. Its unique structure and mechanism of action make it a prominent reagent for researchers investigating the role of neutrophil elastase in both physiological and pathological contexts, particularly those related to inflammation, immune responses, and extracellular matrix dynamics.
Protease inhibition studies: Lonodelestat is widely employed in biochemical experiments to selectively inhibit human neutrophil elastase activity. By providing a means to block this protease with precision, the compound enables researchers to delineate the specific contributions of elastase-mediated proteolysis in complex biological systems. This selective inhibition is instrumental in distinguishing the downstream effects of elastase from those of other proteases, thereby clarifying its role in processes such as cytokine release, chemotaxis, and tissue degradation.
Inflammation and immune response research: The compound's ability to modulate neutrophil elastase activity makes it a critical asset in studies of inflammation and innate immunity. Researchers utilize lonodelestat to model the effects of elastase inhibition on neutrophil-driven inflammatory cascades, including the regulation of cytokine networks, leukocyte migration, and the resolution of inflammatory lesions. These investigations provide mechanistic insights into the interplay between proteases and inflammatory mediators, supporting the development of new hypotheses regarding immune regulation.
Extracellular matrix remodeling assays: In tissue engineering and fibrosis research, lonodelestat is applied to explore the impact of elastase activity on extracellular matrix (ECM) turnover. By inhibiting elastase, investigators can assess its role in the degradation of ECM components such as elastin and collagen. This application is particularly valuable for elucidating the molecular drivers of tissue remodeling, wound healing, and pathological matrix breakdown in fibrotic diseases or chronic inflammatory conditions.
Cell signaling pathway analysis: The compound is also utilized to dissect signal transduction pathways modulated by proteolytic activity. Through the controlled inhibition of neutrophil elastase, researchers can investigate changes in cell surface receptor activation, intracellular signaling cascades, and gene expression profiles. Such studies are essential for understanding how protease activity influences cellular responses, including apoptosis, proliferation, and differentiation, within diverse biological contexts.
Peptide drug development and screening: Lonodelestat serves as a model compound in the development and screening of next-generation peptide-based inhibitors targeting serine proteases. Its well-characterized inhibitory profile provides a benchmark for evaluating the potency, selectivity, and stability of novel peptide therapeutics in preclinical research. By employing lonodelestat as a reference inhibitor, scientists can optimize lead compounds for improved efficacy and specificity, accelerating the rational design of protease-targeting agents for research applications.
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