AMY-101 is a peptidic inhibitor of the central complement component C3.
CAT No: R1905
CAS No:1427001-89-5
Synonyms/Alias:Compstatin 40;AMY-101;1427001-89-5;UNII-4Z4DFR9BX7;4Z4DFR9BX7;peptide 14 [PMID: 22795972];S3,S13-Cyclo(D-tyrolsyl-L-isoleucyl-L-cysteinyl-L-valyl-1-methyl-L-tryptophyl-L-glutaminyl-L-aspartyl-L-tryptophyl-N-methyl-L-glycyl-L-alanyl-L-histidyl-L-arginyl-L-cysteinyl-N-methyl-L-isoleucinamide);CP40;peptide 14 (PMID: 22795972);L-ISOLEUCINAMIDE, D-TYROSYL-L-ISOLEUCYL-L-CYSTEINYL-L-VALYL-1-METHYL-L-TRYPTOPHYL-L-GLUTAMINYL-L-.ALPHA.-ASPARTYL-L-TRYPTOPHYL-N-METHYLGLYCYL-L-ALANYL-L-HISTIDYL-L-ARGINYL-L-CYSTEINYL-N2-METHYL-, CYCLIC (3->13)-DISULFIDE;L-Isoleucinamide, D-tyrosyl-L-isoleucyl-L-cysteinyl-L-valyl-1-methyl-L-tryptophyl-L-glutaminyl-L-alpha-aspartyl-L-tryptophyl-N-methylglycyl-L-alanyl-L-histidyl-L-arginyl-L-cysteinyl-N2-methyl-, cyclic (3->13)-disulfide;C3 Inhibitor AMY-101;Amy 101;AMY101;AMY 101 [WHO-DD];CHEMBL4297260;SCHEMBL24725150;GTPL11986;GLXC-26151;C3 Complement Inhibitor AMY-101;DA-50439;
Chemical Name:2-[(4R,7S,10S,13S,19S,22S,25S,28S,31S,34R)-34-[[(2S,3S)-2-[[(2R)-2-amino-3-(4-hydroxyphenyl)propanoyl]amino]-3-methylpentanoyl]amino]-4-[[(2S,3S)-1-amino-3-methyl-1-oxopentan-2-yl]-methylcarbamoyl]-25-(3-amino-3-oxopropyl)-7-(3-carbamimidamidopropyl)-10-(1H-imidazol-5-ylmethyl)-19-(1H-indol-3-ylmethyl)-13,17-dimethyl-28-[(1-methylindol-3-yl)methyl]-6,9,12,15,18,21,24,27,30,33-decaoxo-31-propan-2-yl-1,2-dithia-5,8,11,14,17,20,23,26,29,32-decazacyclopentatriacont-22-yl]acetic acid
AMY-101 is a synthetic cyclic peptide inhibitor specifically designed to target the complement system, a central component of innate immunity. As a highly selective inhibitor of complement component C3, AMY-101 has become a valuable biochemical tool for dissecting the roles of complement activation in various physiological and pathological processes. Its unique structure and mechanism of action enable precise modulation of complement pathways, making it particularly significant for researchers investigating immune regulation, inflammatory responses, and complement-mediated cellular interactions. The compound's robust performance in preclinical studies has established it as an essential reagent for laboratories focused on immunology, molecular biology, and translational research.
Complement pathway research: AMY-101 is widely utilized in experimental settings to elucidate the function and regulation of the complement system, with a particular emphasis on the central role of C3. By selectively blocking C3 activation, the peptide enables researchers to investigate downstream effects on both the classical and alternative complement pathways. This targeted inhibition provides a powerful approach for mapping complement-mediated signaling events, clarifying the interplay between innate and adaptive immunity, and identifying key regulatory nodes within the cascade.
Inflammation modeling: The compound serves as an effective tool for modeling inflammatory processes in vitro and in vivo. Its ability to suppress complement-driven inflammation allows scientists to distinguish between complement-dependent and independent mechanisms in cellular and tissue models. This facilitates the study of cytokine release, leukocyte recruitment, and other inflammatory mediators, providing insights into the molecular underpinnings of immune-mediated tissue damage and repair.
Autoimmunity and immunopathology studies: AMY-101 is frequently employed in research investigating the contribution of complement activation to autoimmune disorders and immunopathological conditions. By interrupting the amplification loop of complement activation, the peptide enables detailed analysis of how dysregulated complement contributes to the onset and progression of autoimmunity. This application supports the identification of novel biomarkers and therapeutic targets by clarifying the role of C3 in disease-relevant immune responses.
Translational immunology assays: In translational research, AMY-101 is used to bridge fundamental complement biology with clinically relevant models. Its selective inhibition of C3 provides a means to validate hypotheses generated from genetic or observational studies, facilitating the exploration of complement-targeted interventions in preclinical systems. The compound is often incorporated into cell-based assays, organotypic cultures, and ex vivo tissue models to assess complement involvement in disease mechanisms and to inform the development of new diagnostic or therapeutic strategies.
Protein interaction and structure-function analysis: The cyclic peptide structure of AMY-101 offers unique opportunities for studying protein-protein interactions within the complement cascade. Researchers utilize the compound to probe the binding dynamics between C3 and its interacting partners, elucidate structural determinants of complement activation, and develop structure-activity relationships for next-generation inhibitors. These studies contribute to a deeper understanding of complement system architecture and inform the rational design of novel modulators with improved specificity and efficacy.
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