Compstatin

Compstatin is a 13-residue cyclic peptide that inhibits complement activation by binding to complement component C3. It acts as a potent inhibitor of the complement system.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Compstatin(CAS 206645-99-0)

CAT No: R0889

CAS No:206645-99-0

Synonyms/Alias:COMPSTATIN;206645-99-0;CHEMBL266963;CID 16220219;Compstatin?;ICVVQDWGHHRCT-NH2;Compstatin trifluoroacetate salt;GTPL9218;BDBM50241352;AKOS024457182;CCG-270690;AC-33698;FC109863;D80482;Q27076880;H-Ile-Cys-Val-Val-Gln-Asp-Trp-Gly-His-His-Arg-Cys-Thr-NH2; H-ICVVQDWGHHRCT-NH2;

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M.F/Formula
C66H99N23O17S2
M.W/Mr.
1550.8
Sequence
One Letter Code:ICVVQDWGHHRCT
Three Letter Code:H-Ile-Cys(1)-Val-Val-Gln-Asp-Trp-Gly-His-His-Arg-Cys(1)-Thr-NH2
Biological Activity
Complement inhibitor; binds C3 inhibiting proteolytic cleavage by C3 convertase (IC50 = 28 μM) and activation of classical and alternative complement pathways (IC50 values are 63 and 12 μM respectively). Prolongs graft survival and reduces hyperacute rejection of ex vivo pig kidneys perfused with human blood and inhibits in vivo heparin/protamine-induced complement activation in primates.

Compstatin is a synthetic cyclic peptide known for its potent and selective inhibition of the complement system component C3. As a well-characterized complement inhibitor, it has become a valuable tool in immunology and inflammation research, enabling the precise modulation of innate immune responses in a controlled experimental setting. Its unique ability to prevent the activation of C3, a central node in the complement cascade, renders it highly relevant for studies exploring the molecular mechanisms of complement-mediated processes, immune regulation, and disease pathogenesis. The structural stability and specificity of Compstatin also make it a preferred choice for mechanistic investigations and functional assays involving complement biology.

Complement Pathway Studies: Compstatin is widely utilized in research focused on dissecting the complement cascade, particularly at the level of C3 activation. By binding to C3 and preventing its cleavage, the peptide provides researchers with a reliable means to selectively block complement activation and analyze the downstream consequences on immune signaling, cell lysis, and opsonization. This targeted inhibition is instrumental in clarifying the roles of individual complement components and their contributions to innate immunity.

Inflammation Modeling: The peptide's ability to modulate complement activity is especially valuable in experimental models of inflammation. By attenuating complement-mediated inflammatory responses, it allows scientists to delineate the contribution of the complement system to acute and chronic inflammatory processes. This application is crucial for understanding the interplay between complement activation and the recruitment of immune cells, cytokine release, and tissue damage in various disease models.

Protein-Protein Interaction Analysis: Compstatin serves as a model inhibitor for studying the interactions between complement proteins and their regulators or effectors. Its defined binding site on C3 facilitates structural and biophysical studies aimed at elucidating the molecular basis of complement inhibition. Such research supports the development of novel inhibitors and enhances the understanding of protein-protein interactions within the complement system.

Biomarker Validation: In biomarker discovery and validation studies, selective inhibition of complement activation with Compstatin helps clarify the functional relevance of complement-derived biomarkers. By selectively blocking C3 activation, researchers can distinguish between complement-dependent and -independent pathways in disease models, strengthening the interpretation of biomarker data and supporting the identification of new diagnostic or prognostic indicators.

Ex Vivo Functional Assays: The compound is frequently employed in ex vivo systems, such as human plasma or serum assays, to assess complement activity and its modulation under controlled conditions. Its use enables the evaluation of complement-dependent cytotoxicity, opsonization, and immunomodulation in a reproducible manner, providing critical insights into the functional dynamics of the complement system in health and disease. Through these applications, Compstatin has established itself as an indispensable reagent for advancing complement research and immunological studies.

Long-term Storage Conditions
Soluble to 2 mg/ml in water
Shipping Condition
Room temperature in continental US; may vary elsewhere.
InChI
InChI=1S/C66H99N23O17S2/c1-8-32(6)50(68)63(104)86-46-27-108-107-26-45(62(103)89-53(33(7)90)54(69)95)85-56(97)39(14-11-17-74-66(70)71)80-59(100)43(20-36-24-73-29-78-36)83-58(99)42(19-35-23-72-28-77-35)79-48(92)25-76-55(96)41(18-34-22-75-38-13-10-9-12-37(34)38)82-60(101)44(21-49(93)94)84-57(98)40(15-16-47(67)91)81-64(105)51(30(2)3)88-65(106)52(31(4)5)87-61(46)102/h9-10,12-13,22-24,28-33,39-46,50-53,75,90H,8,11,14-21,25-27,68H2,1-7H3,(H2,67,91)(H2,69,95)(H,72,77)(H,73,78)(H,76,96)(H,79,92)(H,80,100)(H,81,105)(H,82,101)(H,83,99)(H,84,98)(H,85,97)(H,86,104)(H,87,102)(H,88,106)(H,89,103)(H,93,94)(H4,70,71,74)/t32-,33+,39-,40-,41-,42-,43-,44-,45-,46-,50-,51-,52-,53-/m0/s1
InChI Key
RDTRHBCZFDCUPW-KWICJJCGSA-N

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