Title: LYP3, a New Bestatin Derivative for Aminopeptidase N Inhibition
Volume: 7
Issue: 1
Author(s): Yepeng Luan, Chunhua Ma, Zhongguo Sui, Xuejian Wang, Jinhong Feng, Ning Liu, Fanbo Jing, Yan Wang, Minyong Li, Hao Fang and Wenfang Xu
Affiliation:
Keywords:
Aminopeptidase N, bestatin, tumorigenesis, A549, ES-2, MDA-MB-231, tumor cells, angiogenesis, metastasis of tumor, met-alloprotease, angiotensin, enkephalin, neovascularization, leukemia, pharmacokinetics, biotransformation, L-serine benzylamine, flash chromatography, acylation, recrystallization, Water Solubility Assay, Lambert-Beer law, APN Inhibition Assay, L-leucine-p-nitroanilide, microsomal amino-peptidase, MMP-2 Inhibition Assay, ma-trix metalloproteinase-2 (MMP-2), MTT Assay, fetal bovine serum, diphenyltetrazolium bromide, mono-hydrochloride salt, APN high-expressed tumor cell line, APN low-expressed tumor cell line, immunostimulating effect
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.
