Lipopolysaccharide removal by a peptide-functionalized surface.

Research paper by Anna A Nilsson, Camilla C Fant, Magnus M Nydén, Krister K Holmberg

Indexed on: 12 Jan '05Published on: 12 Jan '05Published in: Colloids and Surfaces B: Biointerfaces


Five peptides: BPI(85-109); CAP18(106-137); endotoxin inhibitor (EI); GQ33 and GQ33C, derived from lipopolysaccharide (LPS)-binding molecules were investigated for LPS-binding ability with a view to a potential use in extracorporeal therapy. The surface plasmon resonance technique (SPR) was used to monitor the interaction between LPS in solution and the surface-immobilized peptides. The peptides were covalently bound to a model dextran surface via inherent amino groups or via terminally introduced cysteine residues. The results showed that the binding efficacy and binding stability of the peptides varied greatly. The CAP18(106-137) peptide, which exhibited the highest binding efficacy and binding stability, was also immobilized on a poly(ethylene imine)-poly(ethylene glycol) (PEI-PEG) surface through maleimide-terminal PEG. The binding efficacy of the CAP18(106-137) peptide was not significantly affected by the different immobilization methods used in the attachment to a dextran or a PEI-PEG surface. LPS bound selectively to CAP18(106-137) and showed very low unspecific binding to the PEI-PEG surface layer. The EI peptide proved to have a reasonably good binding capacity but a less stable interaction with LPS. The other peptides exhibited much poorer binding efficacy. We believe that the results presented in this work can be of practical value for the development of extracorporeal treatment of patients suffering from septic shock.