FR 179642 is an impurity of Micafungin, a lipopeptide compound that acts as an antifungal agent with activity against Aspergillus and Candida species.
CAT No: Z10-101-162
CAS No:168110-44-9
Synonyms/Alias:1-[(4R,5R)-4,5-Dihydroxy-L-ornithine]-4-[(4S)-4-hydroxy-4-[4-hydroxy-3-(sulfooxy)phenyl]-L-threonine]pneumocandin A0; 1-[(4R,5R)-4,5-Dihydroxy-L-ornithine]-4-[(S)-4-hydroxy-4-[4-hydroxy-3-(sulfooxy)phenyl]-L-threonine]pneumocandin A0; CMICA; FR 133303
FR 179642 is a small-molecule inhibitor recognized for its potent and selective modulation of matrix metalloproteinase (MMP) activity, particularly targeting MMP-2 and MMP-9. As a synthetic compound, it is widely utilized in biochemical investigations exploring extracellular matrix remodeling, cell migration, and related signaling pathways. Its well-characterized inhibitory profile and specificity for gelatinase-type MMPs make it a valuable tool in elucidating the roles of these enzymes in physiological and pathological contexts. Researchers frequently employ FR 179642 to dissect the contribution of MMPs to tissue development, wound healing, and cellular invasiveness in various in vitro and ex vivo model systems.
Enzyme inhibition studies: FR 179642 serves as a robust probe for the selective inhibition of gelatinase activity in biochemical assays. By blocking the catalytic function of MMP-2 and MMP-9, it enables detailed kinetic analyses and structure-activity relationship (SAR) investigations. Researchers can use it to validate assay systems, benchmark novel metalloproteinase inhibitors, and delineate the substrate preferences of specific MMP isoforms. Its high specificity allows for clear differentiation between gelatinase-dependent and independent proteolytic events, thereby refining the interpretation of experimental data in enzyme characterization studies.
Extracellular matrix research: The compound is extensively employed to investigate mechanisms of extracellular matrix (ECM) turnover and remodeling. By inhibiting gelatinase-mediated degradation of ECM components such as collagen and gelatin, FR 179642 provides a means to study the balance between matrix synthesis and breakdown. This application is particularly relevant in exploring the regulation of tissue architecture, cell-matrix interactions, and the molecular underpinnings of fibrosis or tissue repair. Its use facilitates the identification of downstream signaling pathways affected by altered ECM dynamics.
Cell migration and invasion assays: FR 179642 is a critical reagent in cell-based models assessing the invasive and migratory potential of various cell types, including fibroblasts, endothelial cells, and cancer cells. By selectively blocking MMP-2 and MMP-9 activity, it enables researchers to quantify the contribution of gelatinase-dependent proteolysis to cellular movement through artificial matrices or natural tissue barriers. This application supports mechanistic studies on cell motility, metastasis, and angiogenesis, providing valuable insights for basic research and drug discovery programs.
Pathway elucidation in signal transduction: The compound is instrumental in dissecting signaling networks that are modulated by matrix metalloproteinase activity. By serving as a pharmacological inhibitor, FR 179642 allows for the assessment of downstream effects on pathways such as MAPK, PI3K/Akt, and integrin-mediated signaling. Its application in pathway mapping experiments helps clarify the non-proteolytic roles of MMPs and their impact on cellular responses to environmental cues, stress, or growth factors.
Model system validation: Utilization of FR 179642 in organotypic cultures, tissue explants, and engineered three-dimensional matrices enables validation and refinement of experimental models for studying tissue remodeling and disease progression. By providing a controlled means to modulate gelatinase activity, it assists in establishing the causal relationship between MMP function and observed phenotypic changes. This supports the development of more physiologically relevant in vitro systems for hypothesis-driven research and preclinical screening efforts.
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