Conformations of Myoglobin-Derived Peptides at the Air–Water Interface

Cheung, David L.

doi:10.1021/acs.langmuir.5b04619

Cited by 17 publications

(56 citation statements)

References 66 publications

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“…It is also similar to recent simulations of myoglobin-derived peptides, where both compact and globular states were found 33 . The lack of significant tertiary structure change is also seen in the locations of the residues (Figure 7(b)) which are essentially the same as for the NpT simulations.…”

Section: Dce Interfacesupporting

confidence: 90%

“…Recently replica exchange simulations of lysozyme at the water-dichloroethane interface showed that this can adopt a number of conformations of similar free energy 32 . Simulations of peptides derived from myoglobin also found that these exhibit a number of different interfacial conformations, with the preferred orientation for the two peptides investigated being consistent with their differing emulsification behaviour 33 .…”

Section: Introductionmentioning

confidence: 68%

“…While LSZ and αLa are largely found in compact states, the weaker intermolecular interactions in the myoglobin peptides leads to the formation of extended states 33 . Weakening the interactions in LSZ and αLa, for example through reducing some the disulfide bonds, may be used to promote the formation of extended states.…”

mentioning

confidence: 99%

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Adsorption and conformations of lysozyme andα-lactalbumin at a water-octane interface

Cheung

2017

Preprint

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As they contain both hydrophobic and hydrophilic amino acids proteins will readily adsorb onto interfaces between water and hydrophobic fluids such as oil. This adsorption normally causes changes in protein structure, which can result in a loss of protein function and irreversible adsorption, leading to the formation of protein interfacial films. While this can be advantageous in some applications (e.g. food technology) in most cases it limits our ability to exploit protein functionality at interfaces. To understand and control protein interfacial adsorption and function it is necessary to understand the microscopic conformation of proteins at liquid interfaces. In this paper molecular dynamics simulations are used to investigate the adsorption and conformation of two similar proteins, lysozyme and α-lactalbumin, at a water-octane interface. While they both adsorb onto the interface α-lactalbumin does so in a specific orientation, mediated by two amphipathic helices, while lysozyme adsorbs in a non-specific manner. Using replica exchange simulations both proteins are found to possess a number of distinct interfacial conformations, with compact states similar to the solution conformation being most common for both proteins. Decomposing the different contributions to the protein energy at oil-water interfaces, suggests that conformational change for α-lactalbumin, unlike lysozyme, is driven by favourable protein-oil interactions. Revealing these differences between the factors that govern conformational change at interfaces in otherwise similar proteins can give insight into the control of protein interfacial adsorption, aggregation, and function.

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Section: Dce Interfacesupporting

confidence: 90%

Section: Introductionmentioning

confidence: 68%

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Adsorption and conformations of lysozyme andα-lactalbumin at a water-octane interface

Cheung

2017

Preprint

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show abstract

Section: Introductionmentioning

confidence: 68%

“…The Gromos54a7 force field 45 was used for modelling the proteins and along with SPC water 46 . The Gromos family of force fields have been parameterised against solvation free energies for amino acid side chains 45,47 so may be expected to give a good description of the partitioning of these between water and hydrophobic media and have been used in a number of previous studies of proteins at liquid interfaces 20,21,33,48,49 .…”

Section: B Methodologymentioning

confidence: 99%

Adsorption and conformations of lysozyme and α-lactalbumin at a water-octane interface

Cheung

2017

The Journal of Chemical Physics

Self Cite

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As proteins contain both hydrophobic and hydrophilic amino acids, they will readily adsorb onto interfaces between water and hydrophobic fluids such as oil. This adsorption normally causes changes in the protein structure, which can result in loss of protein function and irreversible adsorption, leading to the formation of protein interfacial films. While this can be advantageous in some applications (e.g., food technology), in most cases it limits our ability to exploit protein functionality at interfaces. To understand and control protein interfacial adsorption and function, it is necessary to understand the microscopic conformation of proteins at liquid interfaces. In this paper, molecular dynamics simulations are used to investigate the adsorption and conformation of two similar proteins, lysozyme and α-lactalbumin, at a water-octane interface. While they both adsorb onto the interface, α-lactalbumin does so in a specific orientation, mediated by two amphipathic helices, while lysozyme adsorbs in a non-specific manner. Using replica exchange simulations, both proteins are found to possess a number of distinct interfacial conformations, with compact states similar to the solution conformation being most common for both proteins. Decomposing the different contributions to the protein energy at oil-water interfaces suggests that conformational change for α-lactalbumin, unlike lysozyme, is driven by favourable protein-oil interactions. Revealing these differences between the factors that govern the conformational change at interfaces in otherwise similar proteins can give insight into the control of protein interfacial adsorption, aggregation, and function.

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Supramolecular Protein Assembly Retains Its Structural Integrity at Liquid–Liquid Interface

Sarker

Lee

Gonçalves

et al. 2020

Adv Materials Inter

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Adsorption of globular proteins at liquid–liquid interface results in compromised structures and functionalities to maintain a thermodynamically favorable state. However, the structural behavior of highly symmetrical supramolecular protein assemblies, adsorbed at the liquid–liquid interface, is not well understood. In this study, a model supramolecular protein assembly, E2 protein nanocage, a dodecahedral cage‐structured protein, is studied upon adsorption at the oil–water interface by both theoretical and experimental analyses. Molecular dynamics simulations and force estimation reveal that noncovalent interactions between E2 subunits dominate over the tangential force experienced by E2 at the interface allowing it to retain its structural integrity. Experimental analyses confirm the adsorption of E2 on the liquid–liquid interface with negligible penetration depth. Molecular structural analyses further suggest the structural integrity of the caged structure of E2 at the oil–water interface with minimal change in the tertiary and secondary structures. In conclusion, this study brings new insights into the behavior of highly symmetrical supramolecular protein assemblies at liquid–liquid interface which is important in preserving their functionalities.

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Conformations of Myoglobin-Derived Peptides at the Air–Water Interface

Cited by 17 publications

References 66 publications

Adsorption and conformations of lysozyme andα-lactalbumin at a water-octane interface

Adsorption and conformations of lysozyme andα-lactalbumin at a water-octane interface

Adsorption and conformations of lysozyme and α-lactalbumin at a water-octane interface

Supramolecular Protein Assembly Retains Its Structural Integrity at Liquid–Liquid Interface

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