The extensional viscoelasticity of protein-coated interfaces

Dimitrijev-Dwyer, Mirjana; Middelberg, Anton P. J.

doi:10.1039/c1sm05253e

Cited by 16 publications

(16 citation statements)

References 52 publications

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“…However, two Maxwell elements in parallel (four-parameter model, equation (3.2)) [38], provided excellent fits to the point of maximum stress for all data (black solid lines). Representing the four-parameter Maxwell model in this way allows the contributions of the two Maxwell elements to be visualized.…”

Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

“…This large difference in maximum stress achieved between DAMP1 and DAMP4 is likely to be due to the longer molecule length of DAMP4. The effect of interfacial networking on interfacial rheology of DAMP4 and DAMP1 has been investigated in previous work, by deliberately inducing intermolecular interactions via metal ion-histidine bridging [38]. In the absence of such intermolecular interactions (i.e.…”

Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

“…This is supported by the fact that the extensional moduli of DAMP4 and DAMP1 in the presence of histidine-bridging metal ions, as reported in the previous work, is much greater than in its absence, reported in this current work. The Maxwell model (equation (3.1)) is the simplest of the spring and dashpot-based mechanical models, which were previously discussed in detail in relation to their application to protein interfaces in the extensional strain model [38]. .…”

Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

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Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Dwyer

James

et al. 2013

J. R. Soc. Interface.

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Mixtures of a large, structured protein with a smaller, unstructured component are inherently complex and hard to characterize at interfaces, leading to difficulties in understanding their interfacial behaviours and, therefore, formulation optimization. Here, we investigated interfacial properties of such a mixed system. Simplicity was achieved using designed sequences in which chemical differences had been eliminated to isolate the effect of molecular size and structure, namely a short unstructured peptide (DAMP1) and its longer structured protein concatamer (DAMP4). Interfacial tension measurements suggested that the size and bulk structuring of the larger molecule led to much slower adsorption kinetics. Neutron reflectometry at equilibrium revealed that both molecules adsorbed as a monolayer to the air -water interface (indicating unfolding of DAMP4 to give a chain of four connected DAMP1 molecules), with a concentration ratio equal to that in the bulk. This suggests the overall free energy of adsorption is equal despite differences in size and bulk structure. At small interfacial extensional strains, only molecule packing influenced the stress response. At larger strains, the effect of size became apparent, with DAMP4 registering a higher stress response and interfacial elasticity. When both components were present at the interface, most stress-dissipating movement was achieved by DAMP1. This work thus provides insights into the role of proteins' molecular size and structure on their interfacial properties, and the designed sequences introduced here can serve as effective tools for interfacial studies of proteins and polymers.

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Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

Section: Influence Of Molecule Length On Interfacial Rheologymentioning

confidence: 99%

See 1 more Smart Citation

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Dwyer

James

et al. 2013

J. R. Soc. Interface.

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“…This is despite the fact that the number of AM1 units (four AM1 per S28C) is the same at the concentrations used and may be due to more extensive cross-linking mediated by histidine coordination of Zn 2+ . 53 However, both the two have shown excellent ductile properties that able to resist large strain stretches, as evidenced by the continuous hysteresis curves. The interfacial elastic modulus of the film structure can be calculated from the slope of the initial linear part of the curve, which is described by the equation: 53…”

Section: Mechanical Properties Of Interfacial Protein Networkmentioning

confidence: 99%

“…53 However, both the two have shown excellent ductile properties that able to resist large strain stretches, as evidenced by the continuous hysteresis curves. The interfacial elastic modulus of the film structure can be calculated from the slope of the initial linear part of the curve, which is described by the equation: 53…”

Section: Mechanical Properties Of Interfacial Protein Networkmentioning

confidence: 99%

Droplet shape control using microfluidics and designer biosurfactants

2021

Focus on Surfactants

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Many uses of emulsion droplets require precise control over droplet size and shape. Here we report a 'shape-memorable' micro-droplet formulation stabilized by a polyethylene glycol (PEG)-modified protein-surfactant, the droplets are stable against coalescence for months and can maintain non-spherical shapes for hours, depending on the surface coverage of PEGylated protein. Monodisperse droplets with aspect ratios ranging from 1.0 to 3.4 were controllably synthesized with a flow-focusing microfluidic device. Mechanical properties of the interfacial protein network were explored to elucidate the mechanism behind the droplet shape conservation phenomenon. Characterization of the protein film revealed that the presence of a PEG layer at interfaces alters the mechanical responses of the protein film, resulting in interfacial networks with improved strength. Taking advantage of the prolonged stabilization of non-spherical droplets, we demonstrate the possibility of functionalization of the droplet interface with accessible biotin moieties. The stabilization of micro-droplet shape with surface-active proteins that also serve as an anchor for integrating functional moieties, provides a tailorable interface for diverse applications. File list (2) download file view on ChemRxiv Droplet Shape Control Using Microfluidics and Designer Bi... (1.90 MiB) download file view on ChemRxiv

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Interfaces Between Two Fluids

Langévin

2020

Soft and Biological Matter

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The extensional viscoelasticity of protein-coated interfaces

Cited by 16 publications

References 52 publications

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Insights into the role of protein molecule size and structure on interfacial properties using designed sequences

Droplet shape control using microfluidics and designer biosurfactants

Interfaces Between Two Fluids

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