Molecular simulation of an aerosol OT reverse micelle: 2. Energy and kinetic characteristics

Mudzhikova, G. V.; Brodskaya, E. N.

doi:10.1134/s1061933x0606010x

Cited by 10 publications

(16 citation statements)

References 5 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The results (not shown) indicate an elliptical geometry for the unrestrained RMs that are consistent with the results of previous experimental and simulations studies. 9 − 14 , 24 , 27 , 38 …”

Section: Resultsmentioning

confidence: 99%

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

et al. 2014

View full text Add to dashboard Cite

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.

show abstract

Section: Resultsmentioning

confidence: 99%

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

et al. 2014

View full text Add to dashboard Cite

show abstract

“…An overwhelming majority of computational studies of reverse micellar systems have focused on the anionic Aerosol OT surfactant (sodium bis-(2-ethylhexyl)sulfosuccinate) [37][38][39][40][41][42][43][44][45][46][47] . In re-cent years, however, there has been a surge of studies in which other surfactants and reverse micellar systems have been considered 21,[48][49][50][51][52][53][54][55][56][57][58][59][60] .…”

Section: Introductionmentioning

confidence: 99%

Aggregation response of triglyceride hydrolysis products in cyclohexane and triolein

Vierros

Österberg

Sammalkorpi

2018

Phys. Chem. Chem. Phys.

View full text Add to dashboard Cite

show abstract

“…In this context, computer simulation appears to be a suitable tool to gain a complementary description of these micellar systems at the atomic level. Several computational studies has been performed to analyze nonionic isolated RMs − and AOT RM. − These works have employed different modeling schemes, ranging from mean field approximations to coarse-grained and fully atomistic descriptions of the systems under investigation. In what follows, we will present results from the computer simulation of BHDC RMs.…”

Section: Introductionmentioning

confidence: 99%

Molecular Dynamics Simulation of Water/BHDC Cationic Reverse Micelles. Structural Characterization, Dynamical Properties, and Influence of Solvent on Intermicellar Interactions

2014

View full text Add to dashboard Cite

We report results obtained from molecular dynamics (MD) experiments of benzylhexadecyldimethylammonium chloride (BHDC) cationic reverse micelles (RMs). In particular we analyzed equilibrium and dynamical characteristics of water/BHDC RMs in pure benzene, at two different water/BHDC ratios (W0 = 5 and W0 = 10). The RMs appear as elliptical aggregates with eccentricities close to ∼0.9. Analysis of the different spatial correlations reveals three different spatial domains in the RMs: a water inner pool, the surfactant interface, and the external solvent. The calculated accessible surface areas for the aqueous inner cores suggest a strong penetration of solvent molecules within the micellar interface domains. Comparison between the density profiles of both RMs shows an increment of the broadness in the distributions of all species at the interface, along with an increasing overlap between the tail segments of the surfactant and benzene molecules as one considers larger micelles. For the dynamical side, the rotational characteristic time scale for the confined water was found to be 1 order of magnitude larger than that of the bulk water. A similar effect was also observed for hydrogen bond dynamics. Both retardation effects diminish with the size of the aggregate. To the estimate the influence of the external solvent on the intermicellar interactions, free energy profiles for the coalescence process between RMs of similar size in pure benzene and in a n-heptane/benzene mixture were also investigated. The results indicate that the association process is facilitated by the presence of n-heptane in the external nonpolar phase. Comparison with previous theoretical and experimental results is also carried out.

show abstract

Molecular simulation of an aerosol OT reverse micelle: 2. Energy and kinetic characteristics

Cited by 10 publications

References 5 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

Aggregation response of triglyceride hydrolysis products in cyclohexane and triolein

Molecular Dynamics Simulation of Water/BHDC Cationic Reverse Micelles. Structural Characterization, Dynamical Properties, and Influence of Solvent on Intermicellar Interactions

Contact Info

Product

Resources

About

Molecular simulation of an aerosol OT reverse micelle: 2. Energy and kinetic characteristics

Cited by 10 publications

References 5 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

Aggregation response of triglyceride hydrolysis products in cyclohexane and triolein

Molecular Dynamics Simulation of Water/BHDC Cationic Reverse Micelles. Structural Characterization, Dynamical Properties, and Influence of Solvent on Intermicellar Interactions

Contact Info

Product

Resources

About

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