Aptamer-capture based assays for human neutrophil elastase.
作者： Lin Cheng , Qiang Zhao
DOI: 10.1016/J.TALANTA.2012.11.016
关键词: Proteinase K 、 Elastase 、 Chemistry 、 Aptamer 、 Trypsin 、 Cathepsin G 、 Thrombin 、 Pancreatic elastase 、 Molecular biology 、 Biochemistry 、 Proteinase 3
摘要: Human neutrophil elastase (HNE) is a multifunctional serine protease, involved in infection defense, inflammatory process regulation, and physiopathological processes of several diseases. We developed aptamer-capture based assays for human with different substrates solid supports to meet demands, such as simplicity, sensitivity, high throughput. Aptamers against HNE were immobilized on magnetic beads or microplates affinity ligands capture HNE, then the enriched catalyzed conversion chromogenic fluorogenic products. The measurement generated enzymatic products enabled final detection HNE. In assay using aptamer modified beads, 0.4 pM could be successfully detected. sensitivity was further improved by substrates, limit at 20 fM achieved. use aptamer-coated instead also allowed sensitive offering advantages fast sample handling measurement. established displayed good specificity, proteins including serum albumin, transferrin, immunoglobulin G, thrombin, porcine pancreatic elastase, trypsin, proteinase K, chymotrypsin, lysozyme, cathepsin 3 did not cause interference
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