Polyhydroxyalkanoate chip for the specific immobilization of recombinant proteins and its applications in immunodiagnostics.
Identifieur interne : 003D80 ( Main/Exploration ); précédent : 003D79; suivant : 003D81Polyhydroxyalkanoate chip for the specific immobilization of recombinant proteins and its applications in immunodiagnostics.
Auteurs : Tae Jung Park [Corée du Sud] ; Jong Pil Park [Corée du Sud] ; Seok Jae Lee [Corée du Sud] ; Hyo Jeong Hong [Corée du Sud] ; Sang Yup Lee [Corée du Sud]Source :
- Biotechnology and bioprocess engineering : BBE [ 1226-8372 ] ; 2006.
Abstract
In this study, a novel strategy was developed for the highly selective immobilization of proteins, using the polyhydroxyalkanoate (PHA) depolymerase substrate binding domain (SBD) as an active binding domain. In order to determine the appropriacy of this method for immunodiagnostic assays, the single-chain antibody (ScFv) against the hepatitis B virus (HBV) preS2 surface protein and the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope protein (SCVe) were fused to the SBD, then directly immobilized on PHA-coated slides via microspotting. The fluorescence-labeled HBV antigen and the antibody against SCVe were then utilized to examine specific interactions on the PHA-coated surfaces. Fluorescence signals were detected only at the spotted positions, thereby indicating a high degree of affinity and selectivity for their corresponding antigens/antibodies. Furthermore, we detected small amounts of ScFv-SBD (2.7 ng/mL) and SCVe-SBD fusion proteins (0.6 ng/mL). Therefore, this microarray platform technology, using PHA and SBD, appears generally appropriate for immunodiagnosis, with no special requirements with regard to synthetic or chemical modification of the biomolecules or the solid surface.
DOI: 10.1007/BF02931904
PubMed: 32218672
Affiliations:
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first="Jong Pil" last="Park">Jong Pil Park</name><affiliation wicri:level="1"><nlm:affiliation>1Department of Chemical and Biomolecular Engineering, Bioprocess Engineering Research Center, Center for Ultramicrochemical Process Systems, Korea Advanced Institute of Science and Technology, 305-701 Daejeon, Korea.</nlm:affiliation><country xml:lang="fr">Corée du Sud</country><wicri:regionArea>1Department of Chemical and Biomolecular Engineering, Bioprocess Engineering Research Center, Center for Ultramicrochemical Process Systems, Korea Advanced Institute of Science and Technology, 305-701 Daejeon</wicri:regionArea><wicri:noRegion>305-701 Daejeon</wicri:noRegion></affiliation></author><author><name sortKey="Lee, Seok Jae" sort="Lee, Seok Jae" uniqKey="Lee S" first="Seok Jae" last="Lee">Seok Jae Lee</name><affiliation wicri:level="1"><nlm:affiliation>1Department of Chemical and Biomolecular Engineering, Bioprocess Engineering Research Center, Center for Ultramicrochemical Process Systems, 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type="published">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In this study, a novel strategy was developed for the highly selective immobilization of proteins, using the polyhydroxyalkanoate (PHA) depolymerase substrate binding domain (SBD) as an active binding domain. In order to determine the appropriacy of this method for immunodiagnostic assays, the single-chain antibody (ScFv) against the hepatitis B virus (HBV) preS2 surface protein and the severe acute respiratory syndrome coronavirus (SARS-CoV) envelope protein (SCVe) were fused to the SBD, then directly immobilized on PHA-coated slides via microspotting. The fluorescence-labeled HBV antigen and the antibody against SCVe were then utilized to examine specific interactions on the PHA-coated surfaces. Fluorescence signals were detected only at the spotted positions, thereby indicating a high degree of affinity and selectivity for their corresponding antigens/antibodies. Furthermore, we detected small amounts of ScFv-SBD (2.7 ng/mL) and SCVe-SBD fusion proteins (0.6 ng/mL). Therefore, this microarray platform technology, using PHA and SBD, appears generally appropriate for immunodiagnosis, with no special requirements with regard to synthetic or chemical modification of the biomolecules or the solid surface.</div></front></TEI><affiliations><list><country><li>Corée du Sud</li></country></list><tree><country name="Corée du Sud"><noRegion><name sortKey="Park, Tae Jung" sort="Park, Tae Jung" uniqKey="Park T" first="Tae Jung" last="Park">Tae Jung Park</name></noRegion><name sortKey="Hong, Hyo Jeong" sort="Hong, Hyo Jeong" uniqKey="Hong H" first="Hyo Jeong" last="Hong">Hyo Jeong Hong</name><name sortKey="Lee, Sang Yup" sort="Lee, Sang Yup" uniqKey="Lee S" first="Sang Yup" last="Lee">Sang Yup Lee</name><name sortKey="Lee, Seok Jae" sort="Lee, Seok Jae" uniqKey="Lee S" first="Seok Jae" last="Lee">Seok Jae Lee</name><name sortKey="Park, Jong Pil" sort="Park, Jong Pil" uniqKey="Park J" first="Jong Pil" last="Park">Jong Pil Park</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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