کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1393365 | 1501208 | 2008 | 10 صفحه PDF | دانلود رایگان |

A series of novel pyrrolidine derivatives were designed, synthesized and assayed for their inhibitory activities on matrix metalloproteinase 2 (MMP-2) and aminopeptidase N (AP-N). The results showed that these pyrrolidine derivatives exhibited highly selective inhibition against MMP-2 as compared with AP-N. The hydroxamates 8a–c were equally or more potent MMP-2 inhibitors than the positive control LY52. The binding mode of the most potent compound 8a with MMP-2 was proposed. Structure–activity relationships were also briefly discussed.
A series of novel pyrrolidine derivatives were designed, synthesized and assayed for their inhibitory activities on matrix metalloproteinase 2 (MMP-2) and aminopeptidase N (AP-N). The results showed that these pyrrolidine derivatives exhibited highly selective inhibition against MMP-2 as compared with AP-N. The hydroxamates 8a–c were equally or more potent MMP-2 inhibitors than the positive control LY52. The binding mode of the most potent compound 8a withMMP-2 was proposed. Structure–activity relationships were also briefly discussed.Figure optionsDownload as PowerPoint slide
Journal: European Journal of Medicinal Chemistry - Volume 43, Issue 10, October 2008, Pages 2130–2139