Description of the adsorption behaviour of proteins at water/fluid interfaces in the framework of a two-dimensional solution model

Fainerman, V. B.; Lucassen-Reynders, E. H.; Miller, R.

doi:10.1016/s0001-8686(03)00112-x

Cited by 186 publications

(272 citation statements)

References 58 publications

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“…Dispersion behaviour is known to be affected by the characteristics of interfacial films, and shear rheology is linked to the long-term stability of dispersions, while dilatational rheology provides information regarding short-term stability (32). However, the relationship between interfacial rheological characteristics and dispersion stability is not straightforward (33).…”

Section: Dilatational Measuring Techniquesmentioning

confidence: 99%

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Pelipenko¹,

Kristl²,

Rošic³

et al. 2012

Acta Pharmaceutica

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Colloidal disperse systems represent the increasing number of modern delivery systems whose primary characteristic, a large interfacial area, causes thermodynamic instability. Therefore, the foremost challenge in dispersion design is the reduction of interface instability and an understanding of the behaviour of interfaces. Interfacial rheology is one of the most powerful tools for observing occurrences at the interphase. As previously mentioned, the stability of such systems is provided by the formation of a stable interfacial layer of surfactants around each dispersible particle. The stability of these systems can be improved by using more than one surfactant, but it must be kept in mind that different surfactants can have varying mechanisms of stabilisation, some of which can be mutually incompatible. Surfactant selection is therefore crucial and must be based on physicochemical properties, stability of the interfacial film, mobility of the molecules in the interfacial film, HLB, film formation kinetics, compatibility and interactions between molecules on the surface, CMC, etc. Interfacial rheological properties have yet to be thoroughly explored. Only recently, methods have been introduced that provide sufficient sensitivity to reliably determine viscoelastic interfacial properties. In general, interfacial rheology describes the relationship between the deformation of an interface and the stresses exerted on it.Due to the variety in deformations of the interfacial layer (shear and expansions or compressions), the field of interfacial rheology is divided into the subcategories of shear and dilatational rheology. While shear rheology is primarily linked to the long-term stability of dispersions, dilatational rheology provides information regarding short-term stability. Interfacial rheological characteristics become relevant in systems with large interfacial areas, such as emulsions and foams, and in processes that lead to a large increase in the interfacial area, such as electrospinning of nanofibers.

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Section: Dilatational Measuring Techniquesmentioning

confidence: 99%

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Pelipenko¹,

Kristl²,

Rošic³

et al. 2012

Acta Pharmaceutica

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“…In these models the conformational state of the proteins is often assumed to change with the surface pressure. In the equation of state model of Fainerman et al [13,14], the decrease in apparent size of the adsorbed protein with increasing surface pressure is described as desorption of segments of the protein chain. However, from studies performed with non-unfolding particles (such as Stöber silica particles [15], glass microspheres [16], gelled polymer microbeads [17], latex particles [18], and colloidal silver particles [19]) surface pressure-surface area relations are found that are remarkably similar to those typical for proteins.…”

Section: Introductionmentioning

confidence: 99%

The adsorption and unfolding kinetics determines the folding state of proteins at the air–water interface and thereby the equation of state

Wierenga¹,

Egmond²,

Voragen³

et al. 2006

Journal of Colloid and Interface Science

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Unfolding of proteins has often been mentioned as an important factor during the adsorption process at air-water interfaces and in the increase of surface pressure at later stages of the adsorption process. This work focuses on the question whether the folding state of the adsorbed protein depends on the rate of adsorption to the interface, which can be controlled by bulk concentration. Therefore, the adsorption of proteins with varying structural stabilities at several protein concentrations was studied using ellipsometry and surface tensiometry. For β-lactoglobulin the adsorbed amount (Γ ) needed to reach a certain surface pressure (Π) decreased with decreasing bulk concentration. Ovalbumin showed no such dependence. To verify whether this difference in behavior is caused by the difference in structural stability, similar experiments were performed with cytochrome c and a destabilized variant of this protein. Both proteins showed identical Π-Γ , and no dependence on bulk concentration. From this work it was concluded that unfolding will only take place if the kinetics of adsorption is similar or slower than the kinetics of unfolding. The latter depends on the activation energy of unfolding (which is in the order of 100-300 kJ/mol), rather than the free energy of unfolding (typically 10-50 kJ/mol).

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“…Recently, new theoretical models that include more parameters than the early equations of Langmuir or Gibbs have been developed to describe equilibrium and dynamic aspects of protein adsorption. 32 Monomolecular layers at the air/buffer interface provide a simple method for studying interfacial properties of proteins under controlled conditions. 33 With this technique, we describe surface active properties of mtCK that may contribute to the interaction of this protein with biological or biomimetic membranes.…”

Section: Introductionmentioning

confidence: 99%

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

et al. 2005

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Adsorption to the air/water interface of isoenzymes of creatine kinase was investigated using surface pressure-area isotherms and Brewster angle microscopy (BAM) observations. Octameric mitochondrial creatine kinase (mtCK) exhibits a significant affinity for the air/water interface. Whatever the mode of formation of the interfacial film, i.e., injection of the protein in the subphase or spreading onto the buffer surface, the final arrangement and conformation adopted by mtCK molecules lead to a similar result. In contrast, the dimeric isoenzymes mtCK and cytosolic MMCK do not induce any surface pressure variation. However, when the subphase contains 0.3M NaCl, both isoenzymes adsorb to the interface. When treated with 0.8 or 3M GdnHCl, muscle creatine kinase (MMCK) becomes surface active and occupies a greater surface than mtCK. This result contrasts with previous observations, often derived from monomeric proteins, that their surface activity is increased upon unfolding. It underlines the possible influence exerted by the protein oligomeric state on its interfacial activity. At a subphase pH of 8.8, which corresponds to the pI of octameric mtCK, the profiles of the isotherms obtained with dimeric and octameric states and the resistance to compression of the protein monolayers are significantly affected when compared to those recorded at pH 7.4. These data suggest that the octamer is more hydrophobic than the dimer and may contribute to explaining why octamers bind to the inner mitochondrial membrane while dimers do not.

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Description of the adsorption behaviour of proteins at water/fluid interfaces in the framework of a two-dimensional solution model

Cited by 186 publications

References 58 publications

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

Interfacial rheology: An overview of measuring techniques and its role in dispersions and electrospinning

The adsorption and unfolding kinetics determines the folding state of proteins at the air–water interface and thereby the equation of state

Interfacial behavior of cytoplasmic and mitochondrial creatine kinase oligomeric states

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