MMP-7-IN-3 features a peptide-like inhibitor scaffold used to study matrix metalloproteinase recognition and catalytic-site interactions. Its functional groups enable probing of binding geometry and steric complementarity. Researchers analyze its stability and solvation behavior. Applications include enzymatic profiling, inhibitor optimization, and mechanistic studies.
CAT No: R2510
CAS No:2865097-58-9
Synonyms/Alias:MMP-7-IN-3;CHEMBL5417105;2865097-58-9;BDBM50630413;DA-65559;HY-156430;CS-0901121;
Mmp-7-IN-3 is a small-molecule inhibitor specifically designed to target matrix metalloproteinase-7 (MMP-7), an enzyme implicated in the remodeling of the extracellular matrix and the regulation of various physiological and pathological processes. As a selective MMP-7 inhibitor, this compound plays a pivotal role in mechanistic studies of metalloproteinase function, offering researchers a valuable tool for dissecting the molecular pathways associated with tissue remodeling, inflammation, and cell migration. Its chemical structure allows for high-affinity binding to the catalytic domain of MMP-7, thereby modulating enzymatic activity with precision and enabling detailed exploration of downstream biological effects. Mmp-7-IN-3 is widely utilized in biochemical, cellular, and molecular biology research settings where precise modulation of MMP-7 is required.
Enzyme inhibition studies: Mmp-7-IN-3 serves as a reliable probe for enzymatic assays aimed at characterizing the functional role of MMP-7 in various biological systems. By selectively inhibiting MMP-7 activity, researchers can delineate the specific contributions of this protease to extracellular matrix degradation, cellular signaling, and proteolytic cascades. Such studies are essential for mapping substrate specificity, kinetic parameters, and regulatory mechanisms, providing foundational insights into metalloproteinase biology.
Extracellular matrix research: In investigations of tissue remodeling and matrix turnover, the compound is instrumental for modulating MMP-7-mediated proteolytic activity. Its application enables the study of collagen, elastin, and proteoglycan degradation in cell culture and ex vivo tissue models. By controlling MMP-7 function, scientists can evaluate the consequences of altered matrix dynamics in processes such as wound healing, organ development, and fibrosis, thereby advancing the understanding of matrix homeostasis.
Cell migration and invasion assays: Mmp-7-IN-3 is frequently employed in in vitro assays to assess the role of MMP-7 in cellular motility, invasion, and metastatic potential. By inhibiting the proteolytic remodeling of the extracellular environment, the compound allows for the investigation of how MMP-7 facilitates or restricts cell movement through tissue barriers. These studies are critical for elucidating mechanisms underlying pathological tissue invasion and for identifying molecular checkpoints that govern cell migration.
Inflammation pathway analysis: The selective inhibition of MMP-7 by this compound supports research into inflammatory signaling networks, particularly those involving cytokine activation, chemokine processing, and leukocyte infiltration. By modulating MMP-7 activity, investigators can parse its involvement in the regulation of inflammatory mediators and cellular responses, contributing to a more nuanced understanding of immune system dynamics and the interplay between proteases and inflammation.
Drug discovery and screening: Mmp-7-IN-3 is a valuable reference compound in high-throughput screening platforms and structure-activity relationship (SAR) studies targeting metalloproteinase inhibitors. Its well-characterized inhibitory profile provides a benchmark for evaluating the efficacy and selectivity of novel small molecules. Utilization in early-stage drug discovery workflows supports the identification and optimization of candidate compounds with improved pharmacological properties for research applications focused on metalloproteinase modulation.
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