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Park, Jisoo,Baik Kim, Gae,Lippitz, Andreas,Kim, Young Mi,Jung, Donggeun,Unger, Wolfgang E.S.,Kim, Young-Pil,Lee, Tae Geol Elsevier 2019 Sensors and actuators. B Chemical Vol.281 No.-
<P><B>Abstract</B></P> <P>We report polyethylene glycol (PEG)-grafting antifouling surfaces using a plasma copolymerized (PcP) technique to monitor protease activity in complex media. By varying the mixing ratio of the PEG and ethylenediamine (EDA) precursors, the PcP-PEG-EDA (PcP-PE) film was able to easily control surface amine density with good preservation of the internal PEG structure. We found that nonspecific protein adsorption was dramatically reduced in serum-containing media on the PcP-PE films, as opposed to that on plasma polymerized-EDA (PP-E) films without PEG. When SPR sensor chips coated with PcP-PE film were employed to detect protease activity, biotinylated luciferase probes (luciferase-peptide-biotin) on streptavidin-conjugated SPR chips enabled real-time and label-free measurement of matrix metalloproteinase activity in cell culture media. Owing to its excellent antifouling ability, this newly developed method boasts minimal nonspecific binding and can serve as a biochip platform to promote a wide range of applications in the biological field.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Plasma copolymerized (PcP) method with PEG/EDA created antifoulding surfaces. </LI> <LI> Protease activity in cell culture media was detected on a PcP/SPR sensor chip. </LI> <LI> This approach will be useful for bioassays with minimal nonspecific binding. </LI> </UL> </P>
Peptide-directed Photocrosslinking for Site-specific Conjugation of Native Antibody
Jisoo PARK,Tae Hyeon YOO 한국생물공학회 2021 한국생물공학회 학술대회 Vol.2021 No.10
Antibody-based conjugates have become an essential component in a variety of applications from immunoassays especially to drug conjugates because of their proven efficacy and selectivity to target cancer cell. Herein, we describe a peptide-directed photo-crosslinking reaction as a novel site-specific conjugation method of IgG using an Fc-binding peptide and a photoreactive amino acid analogue for generation homogeneous IgG-toxin conjugates.