Abstract
Aminopeptidase N (APN) is a ubiquitous enzyme overexpressed on tumor cells and plays an important role in angiogenesis and metastasis of tumor. Bestatin as an effective inhibitor of aminopeptidase N is used for complementary treatment of cancer with other drugs. In this work, we reformed the structure of bestatin to a new derivative LYP3 to improve the water solubility and effectiveness. The inhibitory activity of LYP3 against APN was evaluated in vitro.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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CD13 Antigens / antagonists & inhibitors*
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CD13 Antigens / chemistry
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CD13 Antigens / metabolism
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Cell Line, Tumor
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Humans
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Leucine / analogs & derivatives*
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Leucine / chemical synthesis
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Leucine / chemistry
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Leucine / pharmacology
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Matrix Metalloproteinase 2 / chemistry
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Matrix Metalloproteinase 2 / metabolism
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Matrix Metalloproteinase Inhibitors
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Molecular Targeted Therapy
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Neoplasms / drug therapy
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Solubility
Substances
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LYP3 compound
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Matrix Metalloproteinase Inhibitors
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CD13 Antigens
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Matrix Metalloproteinase 2
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Leucine
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ubenimex