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

R. Nigmatullin, R. Lovitt, C. Wright, Markus Linder, Tiina Nakari-Setälä, M. Gama

Research output: Contribution to journalArticleScientificpeer-review

38 Citations (Scopus)

Abstract

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
JournalColloids and Surfaces B: Biointerfaces
Volume35
Issue number2
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

Fingerprint

Atomic Force Microscopy
cellulose
Cellulose
surface reactions
Atomic force microscopy
atomic force microscopy
Surface charge
Electrolytes
interactions
electrolytes
proteins
Proteins
agglomeration
Ionic strength
irregularities
Adhesives
Osmolar Concentration
adhesives
Topography
Peptides

Keywords

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

Cite this

Nigmatullin, R. ; Lovitt, R. ; Wright, C. ; Linder, Markus ; Nakari-Setälä, Tiina ; Gama, M. / Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains. In: Colloids and Surfaces B: Biointerfaces. 2004 ; Vol. 35, No. 2. pp. 125 - 135.
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abstract = "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.",
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Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains. / Nigmatullin, R.; Lovitt, R.; Wright, C.; Linder, Markus; Nakari-Setälä, Tiina; Gama, M.

In: Colloids and Surfaces B: Biointerfaces, Vol. 35, No. 2, 2004, p. 125 - 135.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Atomic force microscopy study of cellulose surface interaction controlled by cellulose binding domains

AU - Nigmatullin, R.

AU - Lovitt, R.

AU - Wright, C.

AU - Linder, Markus

AU - Nakari-Setälä, Tiina

AU - Gama, M.

PY - 2004

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N2 - 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.

AB - 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.

KW - AFM

KW - Colloid probe

KW - Cellulose surface

KW - Cellulose binding domain

KW - Force measurements

U2 - 10.1016/j.colsurfb.2004.02.013

DO - 10.1016/j.colsurfb.2004.02.013

M3 - Article

VL - 35

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EP - 135

JO - Colloids and Surfaces B: Biointerfaces

JF - Colloids and Surfaces B: Biointerfaces

SN - 0927-7765

IS - 2

ER -