COL27A1 inhibitors are a class of chemical compounds specifically designed to target and inhibit the function of the collagen type XXVII alpha 1 (COL27A1) protein. COL27A1 is a unique collagen primarily found in cartilaginous tissues and is particularly important during the development of the skeletal system. This collagen plays a crucial role in the formation of cartilage and bone, contributing to the structural integrity and organization of the extracellular matrix in developing tissues. The protein is characterized by its triple-helical structure, a common feature of collagens, which allows it to form complex fibrillar networks that are essential for maintaining the mechanical properties of cartilage and other connective tissues. COL27A1 is involved in processes such as chondrogenesis and osteogenesis, where it supports the transition from cartilage to bone during skeletal development. Inhibitors of COL27A1 are molecules designed to disrupt these structural roles by binding to specific domains of the protein, thereby affecting its ability to interact with other extracellular matrix components.
The design of COL27A1 inhibitors requires a detailed understanding of the protein's structure and function, particularly the regions involved in its triple-helical formation and interactions with other matrix molecules. These inhibitors are typically small molecules, peptides, or antibodies that exhibit high specificity for COL27A1, binding to critical sites within the protein to prevent it from forming or maintaining its structural networks. The inhibition of COL27A1 can lead to significant alterations in the extracellular matrix, particularly in developing cartilage and bone, where the protein's presence is most prominent. The specificity of these inhibitors is crucial, as COL27A1 shares structural similarities with other collagen types, which necessitates the design of compounds that can distinguish between different collagens to avoid off-target effects. The development of COL27A1 inhibitors involves advanced techniques such as molecular docking, X-ray crystallography, and biochemical assays to identify and refine compounds that effectively target the protein. Additionally, research into COL27A1 inhibitors often includes studying the protein's role in the extracellular matrix, its interaction partners, and the effects of its inhibition on tissue structure and function, ensuring that the inhibitors developed are both potent and selective for COL27A1.
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Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
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L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $45.00 | 5 | |
Essential for the hydroxylation of proline residues in collagen, thus stabilizing the collagen triple helix including COL27A1. | ||||||
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $26.00 $92.00 $120.00 $310.00 $500.00 $908.00 $1821.00 | 46 | |
A tyrosine kinase inhibitor that can alter collagen synthesis by affecting the phosphorylation state of proteins within the pathway. | ||||||
3-Aminopropionitrile | 151-18-8 | sc-266473 | 1 g | $102.00 | ||
Inhibits lysyl oxidase, an enzyme crucial for collagen cross-linking, which can indirectly affect the maturation of COL27A1 fibers. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $45.00 $94.00 | ||
Binds to pyridoxal 5'-phosphate and can disrupt lysyl oxidase activity, leading to less cross-linked and potentially dysfunctional COL27A1. | ||||||
Chloroquine | 54-05-7 | sc-507304 | 250 mg | $68.00 | 2 | |
Raises endosomal pH, which can affect the post-translational modification of collagen and thereby impact COL27A1 stability. | ||||||
Halofuginone | 55837-20-2 | sc-507290 | 100 mg | $1740.00 | ||
An inhibitor of collagen synthesis and can lead to a reduction in the deposition of collagens including COL27A1 in the extracellular matrix. | ||||||
SB 431542 | 301836-41-9 | sc-204265 sc-204265A sc-204265B | 1 mg 10 mg 25 mg | $80.00 $212.00 $408.00 | 48 | |
Inhibits the TGF-beta signaling pathway, which is implicated in the regulation of collagen synthesis including that of COL27A1. |