Publisher's Note: “Protein folding in a reverse micelle environment: The role of confinement and dehydration” [J. Chem. Phys. 134, 055107 (2011)]

Martinez, Anna Victoria; Domı́nguez, Laura; Rivera, Eva; Straub, John E.

doi:10.1063/1.3570829

Cited by 8 publications

(14 citation statements)

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“…Additionally, the shape of unrestrained RMs fluctuated significantly from an initial spherical geometry, facilitating interaction between the dehydrated peptide and the AOT aliphatic tails that appears to be important in stabilizing the peptide's partial helical character. 24 These results are in agreement with experiments 1 as well as previous computational studies. 9,22,23 These prior studies leave a number of critical questions unanswered.…”

Section: Introductionsupporting

confidence: 92%

“…Abel and coworkers 23 obtained similar results for previous simulations of zwitterionic octaalanine peptides in RMs. Martinez and coworkers 24 performed simulations on capped AKA 2 peptide in bulk water and in RMs of w 0 = 6 that were both spherically restrained and unrestrained. For reference RMs of w 0 = 6, spherically restrained and unrestrained with no peptide were simulated.…”

Section: Introductionmentioning

confidence: 99%

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Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles

et al. 2014

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The propensity of peptides to form α-helices has been intensely studied using theory, computation, and experiment. Important model peptides for the study of the coil-to-helix transition have been alanine–lysine (AKA) peptides in which the lysine residues are placed on opposite sides of the helix avoiding charge repulsion while enhancing solubility. In this study, the effects of capped versus zwitterionic peptide termini on the secondary structure of alanine-rich peptides in reverse micelles are explored. The reverse micelles are found to undergo substantial shape fluctuations, a property observed in previous studies of AOT reverse micelles in the absence of solvated peptide. The peptides are observed to interact with water, as well as the AOT surfactant, including interactions between the nonpolar residues and the aliphatic surfactant tails. Computation of IR spectra for the amide I band of the peptide allows for direct comparison with experimental spectra. The results demonstrate that capped AKA2 peptides form more stable α helices than zwitterionic AKA2 peptides in reverse micelles. The rotational anisotropy decay of water is found to be distinctly different in the presence or absence of peptide within the reverse micelle, suggesting that the introduction of peptide significantly alters the number of free waters within the reverse micelle nanopool. However, neither the nature of the peptide termini (capped or charged) nor the degree of peptide helicity is found to significantly alter the balance of interactions between the peptides and the environment. Observed changes in the degree of helicity in AKA2 peptides in bulk solution and in reverse micelle environments result from changes in peptide confinement and hydration as well as direct nonpolar and polar interactions with the water–surfactant interface.

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Section: Introductionsupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles

et al. 2014

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“…Also, both the head groups and counter‐ions lowers the activity of water molecules in RM interior, making the water less available to solvate entrapped BSA. With increasing water loading, we expect that the activity of water increases, allowing for more complete solvation of the BSA and relative stabilization of the coil states . In order to further realize the effect of interaction with the [ProC 3 ][LS] on the secondary structure of the BSA within confined environment, the subsequent analysis of far‐UV CD spectral results has been undertaken.…”

Section: Resultsmentioning

confidence: 99%

Study on the Conformation of Entrapped Protein inside the Reverse Micellar Confinement Based on the Amino Acid Derived Ionic Liquid

et al. 2018

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Owing to superior surface‐activity and versatility in functionalization compared to conventional surfactants, surface‐active ionic liquids (SAILs) gained immense interest in recent years. Toxicity and biodegradation remain central issues while dealing with the SAILs and thus, the quest for synthesis of greener SAILs is increasing day by day. Keeping in view of the importance of SAIL's performance, we undertook the present study for the formulation of reverse micelles (RMs) using biodegradable L‐proline propyl ester lauryl sulfate ([ProC3][LS]) in cyclohexane (Cy). The formation of RMs was confirmed from the phase behavior and dynamic light scattering (DLS) studies. Fourier‐transform infrared spectroscopy (FTIR) study revealed the solvation of anionic head group through H‐bonding by added water. An increased micropolarity and reduced microviscosity were evidenced inside the RM droplets as a function of hydration level. Finally, the encapsulation of BSA protein in RMs was investigated through the fluorescence, circular dichroism and DLS studies, which showed conformation with higher degree of secondary structural content than the native state inside the droplet core at higher hydration. Our results signify the importance of the role of hydration in the function of enzyme or protein molecules in molecular crowding environments. These facts certainly prove the versatility of this kind of organized assemblies to alter their inherent properties simply by changing water content.

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“…29 Experiments in RM are conducted with different solvents. 14,17,18 However, to maintain consistency in the force field and with previous simulations, 26,29,32,33 we use iso-octane as the organic solvent. Simulations are conducted with the parallel molecular dynamics program NAMD.…”

Section: A Simulations Of Ubiquitin-aot Rm Self Assemblymentioning

confidence: 99%

Simulations of the confinement of ubiquitin in self-assembled reverse micelles

Tian

Garcı́a

2011

The Journal of Chemical Physics

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We describe the effects of confinement on the structure, hydration, and the internal dynamics of ubiquitin encapsulated in reverse micelles (RM). We performed molecular dynamics simulations of the encapsulation of ubiquitin into self-assembled protein/surfactant reverse micelles to study the positioning and interactions of the protein with the RM and found that ubiquitin binds to the RM interface at low salt concentrations. The same hydrophobic patch that is recognized by ubiquitin binding domains in vivo is found to make direct contact with the surfactant head groups, hydrophobic tails, and the iso-octane solvent. The fast backbone N-H relaxation dynamics show that the fluctuations of the protein encapsulated in the RM are reduced when compared to the protein in bulk. This reduction in fluctuations can be explained by the direct interactions of ubiquitin with the surfactant and by the reduced hydration environment within the RM. At high concentrations of excess salt, the protein does not bind strongly to the RM interface and the fast backbone dynamics are similar to that of the protein in bulk. Our simulations demonstrate that the confinement of protein can result in altered protein dynamics due to the interactions between the protein and the surfactant.

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Publisher's Note: “Protein folding in a reverse micelle environment: The role of confinement and dehydration” [J. Chem. Phys. 134, 055107 (2011)]

Cited by 8 publications

References 0 publications

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles

Study on the Conformation of Entrapped Protein inside the Reverse Micellar Confinement Based on the Amino Acid Derived Ionic Liquid

Simulations of the confinement of ubiquitin in self-assembled reverse micelles

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Publisher's Note: “Protein folding in a reverse micelle environment: The role of confinement and dehydration” [J. Chem. Phys. 134, 055107 (2011)]

Cited by 8 publications

References 0 publications

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA2 in AOT Reverse Micelles

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA2 in AOT Reverse Micelles

Study on the Conformation of Entrapped Protein inside the Reverse Micellar Confinement Based on the Amino Acid Derived Ionic Liquid

Simulations of the confinement of ubiquitin in self-assembled reverse micelles

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Product

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Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles

Role of Charge and Solvation in the Structure and Dynamics of Alanine-Rich Peptide AKA₂ in AOT Reverse Micelles