Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

R. Nigmatullin*, R. Lovitt, C. Wright, M. Linder, T. Nakari-Setälä, M. Gama

*Corresponding author for this work

Research output: Contribution to journalArticleScientificpeer-review

39 Citations (Scopus)


Colloidal probe microscopy has been used to study the interaction between model cellulose surfaces and the role of cellulose binding domain (CBD), peptides specifically binding to cellulose, in interfacial interaction of cellulose surfaces modified with CBDs. The interaction between pure cellulose surfaces in aqueous electrolyte solution is dominated by double layer repulsive forces with the range and magnitude of the net force dependent on electrolyte concentration. AFM imaging reveals agglomeration of CBD adsorbed on cellulose surface. Despite an increase in surface charge owing to CBD binding to cellulose surface, force profiles are less repulsive for interactions involving, at least, one modified surface. Such changes are attributed to irregularity of the topography of protein surface and non-uniform distribution of surface charges on the surface of modified cellulose. Binding double CBD hybrid protein to cellulose surfaces causes adhesive forces at retraction, whereas separation curves obtained with cellulose modified with single CBD show small adhesion only at high ionic strength. This is possibly caused by the formation of the cross-links between cellulose surfaces in the case of double CBD.

Original languageEnglish
Pages (from-to)125-135
Number of pages11
JournalColloids and Surfaces B: Biointerfaces
Issue number2
Publication statusPublished - 15 May 2004
MoE publication typeA1 Journal article-refereed


  • AFM
  • Cellulose binding domain
  • Cellulose surface
  • Colloid probe
  • Force measurements


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