Phases and phase transition in insoluble and adsorbed monolayers of amide amphiphiles: Specific Characteristics of the condensed phases

Vollhardt, D.

doi:10.1016/j.cis.2014.07.014

Cited by 5 publications

(3 citation statements)

References 96 publications

(165 reference statements)

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“…The results obtained indicate that the formation of a heterogeneous adsorption layer of protein is an intrinsic surface process involving the separation of two-dimensional phases. The coexistence of surface phases has been already observed in the solutions of surfactants 51 and their complexes with DNA. 52 Effects of added denaturants in the bulk The addition of strong denaturants (urea and GuHCl) in the bulk of 3.5 µM lysozyme solution results in an acceleration of adsorption kinetics, and the induction period disappears (Fig.…”

Section: Lysozyme Adsorptionmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 99%

“…The effect is less pronounced than for solutions with urea. These observations can be connected with different mechanisms of the modification of the protein tertiary structure in the bulk by the two denaturants, , where remote amino acid residues prevent complete collapse of the globules to differing extents and thereby with the different resulting protein conformations in the surface layer.…”

Section: Resultsmentioning

confidence: 99%

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Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

et al. 2018

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The application of protein deuteration and high flux neutron reflectometry has allowed a comparison of the adsorption properties of lysozyme at the air-water interface from dilute solutions in the absence and presence of high concentrations of two strong denaturants: urea and guanidine hydrochloride (GuHCl). The surface excess and adsorption layer thickness were resolved and complemented by images of the mesoscopic lateral morphology from Brewster angle microscopy. It was revealed that the thickness of the adsorption layer in the absence of added denaturants is less than the short axial length of the lysozyme molecule, which indicates deformation of the globules at the interface. Two-dimensional elongated aggregates in the surface layer merge over time to form an extensive network at the approach to steady state. Addition of denaturants in the bulk results in an acceleration of adsorption and an increase of the adsorption layer thickness. These results are attributed to incomplete collapse of the globules in the bulk from the effects of the denaturants as a result of interactions between remote amino acid residues. Both effects may be connected to an increase of the effective total volume of macromolecules due to the changes of their tertiary structure, that is, the formation of molten globules under the influence of urea and the partial unfolding of globules under the influence of GuHCl. In the former case, the increase of globule hydrophobicity leads to cooperative aggregation in the surface layer during adsorption. Unlike in the case of solutions without denaturants, the surface aggregates are short and wormlike, their size does not change with time, and they do not merge to form an extensive network at the approach to steady state. To the best of our knowledge, these are the first observations of cooperative aggregation in lysozyme adsorption layers.

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Section: Lysozyme Adsorptionmentioning

confidence: 85%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

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Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

et al. 2018

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Dimethyl sulfoxide in a Langmuir trough

Sorokin,

Maiorova,

Zavalishin

2024

Applied Surface Science

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Applications of Brewster angle microscopy from biological materials to biological systems

Daear¹,

Mahadeo²,

Prenner³

2017

Biochimica et Biophysica Acta (BBA) - Biomembranes

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Brewster angle microscopy (BAM) is a powerful technique that allows for real-time visualization of Langmuir monolayers. The lateral organization of these films can be investigated, including phase separation and the formation of domains, which may be of different sizes and shapes depending on the properties of the monolayer. Different molecules or small changes within a molecule such as the molecule's length or presence of a double bond can alter the monolayer's lateral organization that is usually undetected using surface pressure-area isotherms. The effect of such changes can be clearly observed using BAM in real-time, under full hydration, which is an experimental advantage in many cases. While previous BAM reviews focused more on selected compounds or compared the impact of structural variations on the lateral domain formation, this review provided a broader overview of BAM application using biological materials and systems including the visualization of amphiphilic molecules, proteins, drugs, extracts, DNA, and nanoparticles at the air-water interface.

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Phases and phase transition in insoluble and adsorbed monolayers of amide amphiphiles: Specific Characteristics of the condensed phases

Cited by 5 publications

References 96 publications

Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

Adsorption of Denaturated Lysozyme at the Air–Water Interface: Structure and Morphology

Dimethyl sulfoxide in a Langmuir trough

Applications of Brewster angle microscopy from biological materials to biological systems

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