頁籤選單縮合
題 名 | Identification of Human Plasma Proteins by Trypsin Immobilized Digestion Chip and Electrospray Ionization Tandem Mass Spectrometry |
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作 者 | Yang, Ming-hui; Liao, Jiunn-der; Jong, Shiang-bin; Liao, Pao-chi; Liu, Chia-yuan; Wang, Ming-chen; Grunze, Michael; Tyan, Yu-chang; | 書刊名 | Journal of Medical and Biological Engineering |
卷 期 | 25:2 民94.06 |
頁 次 | 頁81-86 |
分類號 | 410.1644 |
關鍵詞 | Self-assembled monolayers; SAMs; Human plasma proteins; Protein digestion; Surface analysis; Nano-high performance liquid chromatography electrospray ionization tandem mass spectrometry; Nano-HPLC-ESI-MS/MS; |
語 文 | 英文(English) |
英文摘要 | Self-assembled monolayers (SAMs) on coinage metal provide versatile modeling systems for studies of interfacial electron transfer, biological interactions, molecular recognition and other interfacial phenomena. Recently the bonding of enzyme to SAMs of alkanethiols onto Au electrode surfaces was exploited to produce a bio-sensing system. In this work, the attachment of trypsin to a SAMs surface of 11-mercaptoundecanoic acid was achieved using water soluble N-ethyl-N'-(3-dimethylaminopropyl) carbodiimide hydrochloride and N-hydroxysuccinimide as coupling agent. Experimental results have revealed that the XPS C1s core levels at 286.3 and 286.5 eV (C with N), 288.1 eV (Amide bond) and 289.3 eV (Carboxylic acid) illustrate the immobilization of trypsin. These data are also in good agreement with FTIR-ATR spectra for the peaks valued at 1659.4 cm^(-1) (Amide Ⅰ) and 1546.6 cm^(-1) (Amide Ⅱ). Using nano-HPLC-ESI-MS/MS observations, analytical results have demonstrated the human plasma proteins digestion of the immobilized trypsin on the functionalized SAMs surface. For such surfaces, human plasma proteins were digested, which shows the enzyme digestion ability of the immobilized trypsin. The terminal groups of the SAMs structure can be further functionalized with biomolecules or antibodies to develop surface-base diagnostics, biosensors, or biomaterials. |
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