Activity-based targeting of secretory phospholipase A₂ enzymes: A fatty-acid-binding-protein assisted approach

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• 作者：Amir Keshavarz^a ; ^{akeshavarz@ucmerced.edu} ; ^{amir.keshavarz.487@my.csun.edu} ; Ligia Zelaya^a ; Jasmeet Singh^b ; Radha Ranganathan^b ; ^{radha.ranganathan@csun.edu} ; Joseph Hajdu^a ; ¹
• 关键词：Phospholipid syntheses ; Fluorescent phospholipid substrates ; Phospholipase A2 assay
• 刊名：Chemistry and Physics of Lipids
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：202
• 期：Complete
• 页码：38-48
• 全文大小：1218 K
• 卷排序：202

文摘

Syntheses of fluorogenic substrates targeting phospholipase A2 for quantitative detection. Acyl amino group at the sn-1 position blocks phospholipase A1. Small reporter groups to preserve membrane and lipid integrity. Fatty-acid-binding-protein fluorescence assay for enzymological characterization of probes. Activities of phospholipase A2 toward the analogs and unmodified lipids are similar.