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A synthetic complement C1q-like peptide selectively interacts with immune complexes

dc.citation.epage1123en_US
dc.citation.issue12en_US
dc.citation.spage1119en_US
dc.citation.volume20en_US
dc.citation.woscount0
dc.contributor.authorChan, ECen_US
dc.contributor.authorPan, MZen_US
dc.contributor.authorChang, CAen_US
dc.contributor.authorWu, TZen_US
dc.contributor.authorKuo, YBen_US
dc.contributor.department生物科技學系zh_TW
dc.contributor.departmentDepartment of Biological Science and Technologyen_US
dc.date.accessioned2014-12-08T15:47:22Z
dc.date.available2014-12-08T15:47:22Z
dc.date.issued1998-12-01en_US
dc.description.abstractA water-soluble peptide possessing an immune complex selective affinity was synthesized and its primary structure established as: Leu-Glu-Gln-Gly-Glu-Asn-Val-Phe-Leu-Gln-Ala-Thr-Ser-Asp-Asp-Cys. This peptide, designated as C1q-like peptide (CLP), represents a possible immune complex binding epitope of complement C1q. CLP has a hydrophilicity value of 0.21. At 0.5 mu M, it inhibited by 50% natural human C1q from binding to horseradish peroxidase-rabbit anti-peroxidase immune complex. CLP failed to inhibit Staphylococcus aureus protein A from binding monomeric IgG. When coated to a microplate, CLP showed selective binding to the immune complex, and could be used for application in immunochemical detection of immune complex.en_US
dc.identifier.doi10.1023/A:1005368118207en_US
dc.identifier.issn0141-5492en_US
dc.identifier.journalBIOTECHNOLOGY LETTERSen_US
dc.identifier.urihttp://dx.doi.org/10.1023/A:1005368118207en_US
dc.identifier.urihttps://ir.lib.nycu.edu.tw/handle/11536/31751
dc.identifier.wosnumberWOS:000078348200006
dc.language.isoen_USen_US
dc.subjecthuman complement C1q-like peptideen_US
dc.subjectimmune complexen_US
dc.subjecthydrophilicityen_US
dc.titleA synthetic complement C1q-like peptide selectively interacts with immune complexesen_US
dc.typeArticleen_US

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