Macroscopic and Microscopic Interactions Between Albumin and Hydrophilic Surfaces

Oss, Carel J. van; Wu, W.; Giese, R. F.

doi:10.1021/bk-1995-0602.ch006

Cited by 16 publications

(5 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Hence the adsorption process must be accelerated by attractive electrostatic interactions, implying that their contribution to the Gibbs free energy of adsorption should be significant at low ionic strength. If we assume the lysozyme molecule to be a spherical particle of radius R = 2 nm, this contribution can be calculated according to where subscript pws means that the interaction takes place between the protein (medium p) and the Si(Ti)O 2 surface (medium s) through water (w). Superscript el refers to the electrostatic nature of the interaction, ε is the dielectric constant of water and l is the separation between both surfaces.…”

Section: Resultsmentioning

confidence: 99%

“…If we assume the lysozyme molecule to be a spherical particle of radius R ) 2 nm, this contribution can be calculated according to 26 where subscript pws means that the interaction takes place between the protein (medium p) and the Si(Ti)O 2 surface (medium s) through water (w). Superscript el refers to the electrostatic nature of the interaction, is the dielectric constant of water and l is the separation between both surfaces.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Absence of Surface Exclusion in the First Stage of Lysozyme Adsorption Is Driven through Electrostatic Self-Assembly

Ball

Ramsden

1997

J. Phys. Chem. B

View full text Add to dashboard Cite

Adsorption kinetics of hen egg white lysozyme at pH 7.4 onto a Si(Ti)O2 surface were measured at two ionic strengths and under different shear rates by means of optical waveguide lightmode spectroscopy. At low ionic strength, increases of the adsorbed amount linear with time suggest that the adsorption proceeds without surface exclusion. Within the concentration range investigated, the duration of this linear regime was inversely proportional to the bulk concentration. The linear regime always stopped at a threshold value of 0.18 ± 0.02 μg/cm2 and was followed by a second regime with surface exclusion. At high ionic strength the linear regime was not observed, suggesting an electrostatically driven self-assembly process at low ionic strength. This conclusion is supported by the linear arrays of lysozyme at graphite surfaces observed with STM (Haggerty, L.; Lenhoff, A. M. Biophys. J. 1993, 64, 886). Moreover, the adsorption rate at low ionic strength is faster than that predicted by diffusion across the diffusion boundary layer, suggesting that the transport is accelerated by electrostatic attraction. This was confirmed by an estimation of the electrostatic free energy contribution.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Absence of Surface Exclusion in the First Stage of Lysozyme Adsorption Is Driven through Electrostatic Self-Assembly

Ball

Ramsden

1997

J. Phys. Chem. B

View full text Add to dashboard Cite

show abstract

“…base (polar) interactions into account led to significant improvement (3), but only when the microscopic geometry of the protein was explicitly included in the energy computation Effect of Phosphate Buffer was the agreement between theory and experiment satisfac-PBS has two striking effects: (i) adsorption is decelerated tory (31). In general, the entropic and enthalpic contribution (k a is reduced by about an order of magnitude) and desorpfrom internal structural rearrangements of the protein (23) tion is accelerated (Table 1); in the case of HSA the irreversand of the surface, if soft (32), must also be included.…”

Section: Competing Reversible/irreversible Adsorptionmentioning

confidence: 99%

Kinetics of Human and Bovine Serum Albumin Adsorption at Silica–Titania Surfaces

Kurrat

Prenosil

Ramsden

1997

Journal of Colloid and Interface Science

171

162

View full text Add to dashboard Cite

“…5 Once the protein is adsorbed, the second step is thought to involve a conformational change that maximizes electrostatic interactions, local interactions between electron donor moieties in the protein with electron acceptors on the surface, and maximization of van der Waals attractions. 6 It is often assumed that this second step involves changes in the protein structure, akin to denaturation. There is now some experimental evidence that "compact" globular proteins maintain their native structure when adsorbed and that only some "soft/flexible" proteins suffer some degree of denaturation upon adsorption, especially on hydrophobic surfaces.…”

Section: Introductionmentioning

confidence: 99%

Imaging the Molecular Dimensions and Oligomerization of Proteins at Liquid/Solid Interfaces

et al. 1998

View full text Add to dashboard Cite

Individual Concanavalin A (ConA) molecules have been imaged at the liquid/solid interface with an atomic force microscope (AFM). Three-dimensional sizing with very high resolution (<5 Å) has been obtained by a novel approach based on height distributions, which avoids the tip convolution effects which normally affect scanning probe microscopy techniques. Each height measurement correlates to a particular molecular orientation on the surface. A large number of such measurements provide a statistical ensemble of orientations. The complete height distribution reflects the three-dimensional size of the protein sample and hence its tertiary and quaternary structure. A surface adsorption and orientation model, based on a minimization of surface adsorption energy, is proposed. This model is in good agreement with the observed height distribution of Con A molecules at the liquid/solid interface. Analysis of Con A and succinylated Con A molecules on mica demonstrates that Con A dimers are the prevalent species at the liquid/solid interface. This is in contrast to the tetrameric organization of Con A normally observed in solution. The new possibilities opened by height distribution analysis on the physical characterization of biomolecules at interfaces are also discussed.

show abstract

Macroscopic and Microscopic Interactions Between Albumin and Hydrophilic Surfaces

Cited by 16 publications

References 0 publications

Absence of Surface Exclusion in the First Stage of Lysozyme Adsorption Is Driven through Electrostatic Self-Assembly

Absence of Surface Exclusion in the First Stage of Lysozyme Adsorption Is Driven through Electrostatic Self-Assembly

Kinetics of Human and Bovine Serum Albumin Adsorption at Silica–Titania Surfaces

Imaging the Molecular Dimensions and Oligomerization of Proteins at Liquid/Solid Interfaces

Contact Info

Product

Resources

About