Thrombospondin (TSP-1)-derived CD36 binding motif

Thrombospondin (TSP-1)-derived CD36 binding motif features a defined peptide sequence used to examine receptor-recognition elements. Charged and hydrophobic residues contribute to structured interaction patterns. Researchers investigate its behavior to understand ligand docking and molecular specificity. Applications span structural biology, peptide engineering, and receptor-binding studies.

Designed for biological research and industrial applications, not intended for individual clinical or medical purposes.
Thrombospondin (TSP-1)-derived CD36 binding motif(CAS 138849-26-0)

CAT No: R2641

CAS No:138849-26-0

Synonyms/Alias:Thrombospondin (TSP-1)-derived CD36 binding motif;EX-A9857;HY-P5322;CS-0881184;138849-26-0;

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M.F/Formula
C20H34N6O9S2
M.W/Mr.
566.7
Sequence
One Letter Code:CSVTCG
Three Letter Code:H-Cys(1)-Ser-Val-Thr-Cys(1)-Gly-OH

Thrombospondin (TSP-1)-derived CD36 binding motif is a specialized carbohydrate compound that has garnered significant interest within the biomedical research community due to its unique ability to interact with the CD36 receptor. This motif, originally identified as a functional domain within the larger thrombospondin-1 glycoprotein, plays a crucial role in mediating various cellular processes through its specific binding affinity. Researchers value this compound for its potential to modulate cell signaling pathways, influence cell-matrix interactions, and regulate physiological as well as pathological processes. Its structural precision enables targeted studies, making it an indispensable tool for probing the mechanisms underlying cellular adhesion, migration, and signal transduction events associated with CD36.

Angiogenesis Research: The TSP-1-derived CD36 binding motif is extensively utilized in angiogenesis studies, particularly for investigating the regulation of new blood vessel formation. By mimicking the natural inhibitory action of thrombospondin-1 fragments on endothelial cells, this motif allows researchers to dissect the molecular mechanisms that suppress angiogenic responses. It serves as a valuable probe for elucidating how CD36-mediated signaling pathways contribute to the inhibition of endothelial cell proliferation, migration, and tube formation, thereby providing insights into the balance between pro- and anti-angiogenic factors in both physiological and pathological contexts.

Atherosclerosis and Lipid Metabolism: In the realm of cardiovascular research, the CD36 binding motif is instrumental in exploring the cellular mechanisms underlying atherosclerosis and lipid metabolism. Its interaction with CD36 on macrophages and other vascular cells enables detailed studies on the uptake of oxidized low-density lipoproteins (oxLDL) and the subsequent formation of foam cells. By applying this motif in cell-based assays, scientists can unravel the complex signaling events that govern lipid accumulation, inflammation, and plaque development, ultimately advancing the understanding of cardiovascular disease progression.

Cell Adhesion and Migration Studies: The TSP-1-derived motif is also pivotal in research focusing on cell adhesion and migration. Its ability to engage CD36 facilitates the examination of how cells interact with their extracellular environment and respond to mechanical and chemical cues. This application is particularly relevant for investigations into wound healing, tissue remodeling, and metastasis, where cell motility and adhesion dynamics are critical. By incorporating the motif into in vitro and ex vivo models, researchers can assess the influence of CD36-mediated pathways on cellular behavior and identify potential modulators of these processes.

Immunomodulation and Inflammation: Another important application of the CD36 binding motif lies in the study of immune cell function and inflammatory responses. Through its specific engagement with CD36 on monocytes, macrophages, and other immune cells, the motif provides a platform for dissecting the regulation of cytokine production, phagocytosis, and cellular activation. This enables a deeper understanding of how thrombospondin-1 fragments influence innate immunity and chronic inflammatory conditions, offering valuable insights into the interplay between extracellular matrix components and immune signaling networks.

Cancer Biology and Tumor Microenvironment: The TSP-1-derived CD36 binding motif is increasingly employed in cancer research to investigate its effects on tumor cell behavior and the tumor microenvironment. By modulating CD36-dependent pathways, the motif allows scientists to probe the mechanisms by which thrombospondin-1 influences tumor angiogenesis, metastasis, and interactions with stromal cells. Its application in co-culture systems and three-dimensional tumor models supports the identification of novel targets for therapeutic intervention and enhances the understanding of how extracellular matrix-derived signals contribute to cancer progression and resistance.

In summary, the Thrombospondin (TSP-1)-derived CD36 binding motif serves as a powerful investigative tool across a diverse array of research fields, including angiogenesis, cardiovascular disease, cell migration, immunology, and oncology. Its precise molecular interactions with CD36 enable the dissection of complex signaling pathways and cellular processes, thereby facilitating the development of innovative experimental models and advancing fundamental knowledge in biomedical science. The versatility and specificity of this carbohydrate compound continue to drive its adoption in cutting-edge research, highlighting its significance in unraveling the molecular basis of health and disease.

InChI
InChI=1S/C20H34N6O9S2/c1-8(2)14-19(34)26-15(9(3)28)20(35)24-12(17(32)22-4-13(29)30)7-37-36-6-10(21)16(31)23-11(5-27)18(33)25-14/h8-12,14-15,27-28H,4-7,21H2,1-3H3,(H,22,32)(H,23,31)(H,24,35)(H,25,33)(H,26,34)(H,29,30)/t9-,10+,11+,12+,14+,15+/m1/s1
InChI Key
BKKZTICNTWDYCN-YLHZTVIJSA-N

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