Abstract
This study demonstrates that synthetic isopeptides formed on BSA can be quantitatively analyzed by a surface plasmon resonance-based biosensor method. A monoclonal IgM antibody 81D4, that reacts with the synthetic isopeptide and also with the natural isopeptide cross-link in D-dimer (but not with its non-cross-linked fibrin monomer), was covalently immobilized to a carboxymethylated dextran surface, a CM5 surface. Its immunocapturing efficiency was found to be good. The affinity of the interaction between the monoclonal 81D4 and the synthetic isopeptide was estimated to approximately 4 × 10-7 M. Good reactivity was also observed when human plasma spiked with this isopeptide was used as test solution. Cross-linked D-dimer in the plasma of patients is a marker of disseminated intravascular coagulation (DIC) which occurs late in sepsis. This biosensor method has the potential to be developed into a rapid sensitive assay for measuring the level of natural isopeptide cross-links in proteins in the plasma of patients with a suspected diagnosis of sepsis.
Original language | English |
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Pages (from-to) | 150-153 |
Number of pages | 4 |
Journal | Colloids and Surfaces B: Biointerfaces |
Volume | 66 |
Issue number | 1 |
DOIs | |
Publication status | Published - 1 Oct 2008 |
Externally published | Yes |
Keywords
- SPR
- Surface plasmon resonance
- Isopeptides
- DIC
- Disseminated intravascular coagulation
- Sepsis
- Optical biosensor assay