Functional characterisation of Fab'-fragments self-assembled onto hydrophilic gold surfaces

Willem M. Albers (Corresponding Author), Sanna Auer, Hannu Helle, Tony Munter, Inger Vikholm-Lundin

Research output: Contribution to journalArticleScientificpeer-review

14 Citations (Scopus)


Antibody Fab′-fragments have been immobilised on hydrophilic gold by direct self-assembly, and embedded in a matrix of non-ionic hydrophilic polymers, tris(hydroxymethyl)methylacrylamide, carrying lipoate terminal linking groups. Different polymers were synthesised, and co-adsorbed or post-adsorbed between the antibody fragments in order to optimise the antigen binding. Various factors were investigated that influence the activity of the immobilised Fab′-fragments for binding of the antigen, human IgG. The Fab′-fragments were immobilised in dense layers close to monolayer coverage, and the stoichiometric efficiency of immobilisation was up to 30%, with the human IgG also approaching monolayer coverage. The cleaning of the gold surface was a crucial factor in preservation of activity. Besides the usual treatment in hot ammonia/peroxide solution, hot DMSO appeared to be highly effective as a cleaning agent.
Original languageEnglish
Pages (from-to)193-199
JournalColloids and Surfaces B: Biointerfaces
Issue number2
Publication statusPublished - 2009
MoE publication typeA1 Journal article-refereed


  • Immunoassay
  • Heterogeneous binding
  • Surface plasmon resonance
  • Antibody Fab'-fragment
  • Immobilisation


Dive into the research topics of 'Functional characterisation of Fab'-fragments self-assembled onto hydrophilic gold surfaces'. Together they form a unique fingerprint.

Cite this