Covalent attachment of functionalized cardiolipin on a biosensor gold surface allows repetitive measurements of anticardiolipin antibodies in serum

Alice Schlichtiger, Claudia Baier, Meng Xin Yin, Andrew B. Holmes, Makiko Maruyama, Ralf Strasser, Ulrich Rant, Markus Thaler, Peter B. Luppa

Research output: Contribution to journalArticlepeer-review

17 Scopus citations

Abstract

Antiphospholipid antibodies (aPL) are a relevant serological indicator of antiphospholipid syndrome (APS). A solid-state surface with covalently bound ω-amine-functionalized cardiolipin was established and the binding of β2-glycoprotein I (β2-GPI) was investigated either by use of surface plasmon resonance (SPR) biosensor, by electrically switchable DNA interfaces (switchSENSE) and by scanning tunneling microscopy (STM). STM could clearly visualize the attachment of β2-GPI to the cardiolipin surface. Using the switchSENSE sensor, β2-GPI as specific ligand could be identified by increased hydrodynamic friction. The binding of anti-cardiolipin antibodies (aCL) was detected against the ω-amine-functionalized cardiolipin-modified SPR biosensor (aCL biosensor) using sera from healthy donors, APS patients and syphilis patients. Our results showed that the aCL biosensor is a much more sensitive diagnostic device for APS patients compared to previous methods. The specificity between β2-GPI-dependent autoimmune- and β2-GPI- independent infection-associated types of aPLs was also studied and they can be distinguished by the different binding kinetics and patterns.

Original languageEnglish
Pages (from-to)275-285
Number of pages11
JournalAnalytical and Bioanalytical Chemistry
Volume405
Issue number1
DOIs
StatePublished - Jan 2013

Keywords

  • Antiphospholipid antibody
  • Antiphospholipid syndrome
  • Cardiolipin
  • Phospholipid
  • Surface plasmon resonance
  • β2-glycoprotein I

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