In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and d...In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and disposable polydimethylsiloxane （PDMS） using a silane-based chemical modification protocol, which yield antibody- terminated PDMS surfaces. In this study, the IX IP device is specifically designed for the purification of carbonylated protein, a representative example here to illustrate the potential applications for any other PTMs, which could be immuno-tagged by specific antibodies. The test model in vitro oxidized bovine serum albumin （BSA） was first derivitized by dinitrophenylhydrazide （DNPH） and then captured by the anti-DNP immobilized on this Ix lP device. The surface functional group mapping was systematically analyzed and validated by fluorescence microscopy. Quantitative study of DNP-derivatized carbonylated protein capture recovery and elution efficiency of the device was also studied. We also envision that this proteome enrichment Ix IP device can be assembled with other lab-on-a-chip components, such as microelectrophoresis or micro-chromatographic devices for follow-up protein analysis. This selective enrichment of modified proteins greatly facilitates the study of low abundant protein biomarkers discovery.展开更多
β-Di-substituted α-amino acids(AAs) contain adjacent carbon stereogenic centers and pose considerable synthetic challenge. Complementary to the conventional synthesis strategies based on the transformation of existi...β-Di-substituted α-amino acids(AAs) contain adjacent carbon stereogenic centers and pose considerable synthetic challenge. Complementary to the conventional synthesis strategies based on the transformation of existing functional groups, we envisioned these molecules could be quickly accessed via selective functionalization of sp3 hybridized C-H bonds on the side chains of common α-AA precursors. We report a readily applicable method to prepare β-alkynyl α-amino acids via Pd-catalyzed diastereoselective C(sp3)-H alkynylation of common α-amino acids precursors with acetylene bromide.展开更多
We prepare oligothymonucleic acid (OTA) functionalized polyethylene (PE) film and evaluate its selective removal ability of mercury ions at ultra-low levels in aqueous solution. The selective binding of OTA with mercu...We prepare oligothymonucleic acid (OTA) functionalized polyethylene (PE) film and evaluate its selective removal ability of mercury ions at ultra-low levels in aqueous solution. The selective binding of OTA with mercury ions is confirmed by fluorescence in situ hybridization (FISH). The quantitative results via cold-vapor atomic fluorescence spectrometry (CVAFS) indicate that OTA-functionalized PE film is able to remove mercury ions at the sub-ppb level selectively from aqueous solution, even with the coexistence of other metal ions at concentrations 250-fold or higher than that of mercury.展开更多
基金National Institutes of Health and the National Center for Research Resources grant number: P20RR01645 and NIH grant # DK44510
文摘In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and disposable polydimethylsiloxane （PDMS） using a silane-based chemical modification protocol, which yield antibody- terminated PDMS surfaces. In this study, the IX IP device is specifically designed for the purification of carbonylated protein, a representative example here to illustrate the potential applications for any other PTMs, which could be immuno-tagged by specific antibodies. The test model in vitro oxidized bovine serum albumin （BSA） was first derivitized by dinitrophenylhydrazide （DNPH） and then captured by the anti-DNP immobilized on this Ix lP device. The surface functional group mapping was systematically analyzed and validated by fluorescence microscopy. Quantitative study of DNP-derivatized carbonylated protein capture recovery and elution efficiency of the device was also studied. We also envision that this proteome enrichment Ix IP device can be assembled with other lab-on-a-chip components, such as microelectrophoresis or micro-chromatographic devices for follow-up protein analysis. This selective enrichment of modified proteins greatly facilitates the study of low abundant protein biomarkers discovery.
基金supported by the Pennsylvania State University and Natural Science Foundation(CAREER CHE-1055795)
文摘β-Di-substituted α-amino acids(AAs) contain adjacent carbon stereogenic centers and pose considerable synthetic challenge. Complementary to the conventional synthesis strategies based on the transformation of existing functional groups, we envisioned these molecules could be quickly accessed via selective functionalization of sp3 hybridized C-H bonds on the side chains of common α-AA precursors. We report a readily applicable method to prepare β-alkynyl α-amino acids via Pd-catalyzed diastereoselective C(sp3)-H alkynylation of common α-amino acids precursors with acetylene bromide.
基金supported by National Natural Science Foundation of China(11175234, 11105210)the Knowledge Innovation Program of the Chinese Academy of Sciences (XDA02040300, KJCX2-YW-N49)Shanghai Municipal Commission for Science and Technology (10ZR1436700,11ZR1445400)
文摘We prepare oligothymonucleic acid (OTA) functionalized polyethylene (PE) film and evaluate its selective removal ability of mercury ions at ultra-low levels in aqueous solution. The selective binding of OTA with mercury ions is confirmed by fluorescence in situ hybridization (FISH). The quantitative results via cold-vapor atomic fluorescence spectrometry (CVAFS) indicate that OTA-functionalized PE film is able to remove mercury ions at the sub-ppb level selectively from aqueous solution, even with the coexistence of other metal ions at concentrations 250-fold or higher than that of mercury.
