Hydrophobins: proteins with potential

Hektor, Harm J.; Scholtmeijer, Karin

doi:10.1016/j.copbio.2005.05.004

Cited by 163 publications

(136 citation statements)

References 48 publications

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“…Due to advances in the synthesis of particles, it is now possible to create particles with anisotropic ''patchy'' or ''Janus'' surface characteristics. 13 Some proteins, for example fungi hydrophobin, 14 also have such an amphiphilic structure. This added complexity allows self-assembly to reach a higher level, with amphiphilic Janus particles assembling into a variety of supracolloidal structures, 15,16 with or without the aid of soft interfaces.…”

Section: 12mentioning

confidence: 99%

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Stability of Janus nanoparticles at fluid interfaces

Cheung

Bon

2009

Soft Matter

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Using Monte Carlo simulations the interaction of a nanometre-sized, spherical Janus particle (a particle with two distinct surface regions of different functionality, in this case showing amphiphilic behaviour) with an ideal fluid interface is studied. In common with previous simulations of spherical, isotropic particles, the range of the nanoparticle-interface interaction is significantly larger than the nanoparticle radius due to the broadening of the interface due to capillary waves. For a uniform particle (an isotropic particle with one surface characteristic) the stability of the particle at a liquid interface is decreased as the affinity for one liquid phase is increased relative to the other; for large affinity differences the detachment energies calculated from continuum theory become increasingly accurate. For a symmetric Janus particle (where the two different surface regions are of equal area), the presence of the particle at the interface becomes more stable upon increasing the difference in affinity between the two faces, with each face having a high affinity for the respective liquid phase. In the case studied here, where surface tension between the A-region of the particle with the A-component is identical to the surface tension between the B-region and B-component, the interaction is symmetric with respect to the nanoparticle interface separation. The particle is found to have a large degree of orientational freedom, in sharp contrast to micrometre-sized colloidal particles. Comparison with continuum theory shows that this significantly overestimates the detachment energy, due to its neglect of nanoparticle rotation; simulations of nanoparticles with fixed orientations show a considerably larger detachment energy. As the areas of the surface regions become asymmetric the stability of the Janus nanoparticle is decreased and, in the case of large differences in affinities of the two faces, the difference between detachment energies from simulation and continuum theory diminishes.

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Section: 12mentioning

confidence: 99%

“…When the particle is in the bulk of the Acomponent the surface free energy is then . (14) The detachment energies eqn (8) are then found by subtraction of eqn (12) from eqn (13) and eqn (14) and recalling that a ¼ b.…”

mentioning

confidence: 99%

Stability of Janus nanoparticles at fluid interfaces

Cheung

Bon

2009

Soft Matter

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“…Many of them involve the adsorption of hydrophobins to modify surfaces (Janssen et al, 2002). The self-assembly of hydrophobins (Wosten and Wessels, 1997) makes them interesting for using as stabilizers of emulsions (Wosten et al, 1994), foaming agents (Hektor and Scholtmeijer, 2005) and targets for the immobilization of other components (Linder, 2009). The application of hydrophobins in biosensor developments (Bilewicz et al, 2001), and in tissue engineering (Janssen et al, 2002) were studied as well.…”

Section: Introductionmentioning

confidence: 99%

A novel method for hydrophobin extraction using CO2 foam fractionation system

Khalesi¹,

Venken

Deckers³

et al. 2013

Industrial Crops and Products

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“…However, only a few protein assemblies form lattices indefinitely extended along two dimensions (2D). Examples of natural self-assembling protein sheets include S-layers of archea and many bacteria (12) and hydrophobin coatings of many fungi (13,14). In addition, self-assembling 2D lattices have been created by engineering other proteins (15)(16)(17)(18).…”

Section: Introductionmentioning

confidence: 99%

Kinetics of Surface-Driven Self-Assembly and Fatigue-Induced Disassembly of a Virus-Based Nanocoating

Valbuena

Mateu

2017

Biophysical Journal

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Self-assembling protein layers provide a ''bottom-up'' approach for precisely organizing functional elements at the nanoscale over a large solid surface area. The design of protein sheets with architecture and physical properties suitable for nanotechnological applications may be greatly facilitated by a thorough understanding of the principles that underlie their self-assembly and disassembly. In a previous study, the hexagonal lattice formed by the capsid protein (CA) of human immunodeficiency virus (HIV) was self-assembled as a monomolecular layer directly onto a solid substrate, and its mechanical properties and dynamics at equilibrium were analyzed by atomic force microscopy. Here, we use atomic force microscopy to analyze the kinetics of self-assembly of the planar CA lattice on a substrate and of its disassembly, either spontaneous or induced by materials fatigue. Both selfassembly and disassembly of the CA layer are cooperative reactions that proceed until a phase equilibrium is reached. Self-assembly requires a critical protein concentration and is initiated by formation of nucleation points on the substrate, followed by lattice growth and eventual merging of CA patches into a continuous monolayer. Disassembly of the CA layer showed hysteresis and appears to proceed only after large enough defects (nucleation points) are formed in the lattice, whose number is largely increased by inducing materials fatigue that depends on mechanical load and its frequency. Implications of the kinetic results obtained for a better understanding of self-assembly and disassembly of the HIV capsid and protein-based two-dimensional nanomaterials and the design of anti-HIV drugs targeting (dis)assembly and biocompatible nanocoatings are discussed.

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Hydrophobins: proteins with potential

Cited by 163 publications

References 48 publications

Stability of Janus nanoparticles at fluid interfaces

Stability of Janus nanoparticles at fluid interfaces

A novel method for hydrophobin extraction using CO2 foam fractionation system

Kinetics of Surface-Driven Self-Assembly and Fatigue-Induced Disassembly of a Virus-Based Nanocoating

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