scholarly journals Linear Free Energy Relationship Correlations for Room Temperature Ionic Liquids: Revised Cation-Specific and Anion-Specific Equation Coefficients for Predictive Applications Covering a Much Larger Area of Chemical Space

2009 ◽  
Vol 48 (8) ◽  
pp. 4145-4154 ◽  
Author(s):  
Laura M. Sprunger ◽  
Jennifer Gibbs ◽  
Amy Proctor ◽  
William E. Acree, Jr. ◽  
Michael H. Abraham ◽  
...  
Keyword(s):  
Free Energy ◽  
Ionic Liquids ◽  
Room Temperature ◽  
Chemical Space ◽  
Room Temperature Ionic Liquids ◽  
Linear Free Energy Relationship ◽  
Linear Free Energy ◽  
Specific Equation

scholarly journals Computational Analysis of the Effect of [Tea][Ms] and [Tea][H2PO4] Ionic Liquids on the Structure and Stability of Aβ(17-42) Amyloid Protofibrils

2020 ◽  
Author(s):  
Dorothea Gobbo ◽  
Andrea Cavalli ◽  
Pietro Ballone ◽  
Antonio Benedetto
Keyword(s):  
Free Energy ◽  
Ionic Liquids ◽  
Room Temperature ◽  
Computational Analysis ◽  
Experimental Studies ◽  
Room Temperature Ionic Liquids ◽  
Organic Salts ◽  
Structure And Stability ◽  
Physiological Conditions ◽  
The Stability

<div>Experimental studies have reported the possibility of affecting the growth/dissolution of amyloid fibres by the addition of organic salts of the room-temperature ionic-liquids family, raising the tantalizing prospect of controlling these processes at physiological conditions. The effect of [Tea][Ms] and [Tea][H2PO4] at various concentrations on the structure and stability of a simple model of Aβ42 fibrils has been investigated by computational means. Free energy computations show that both [Tea][Ms] and [Tea][H2PO4] decrease the stability of fibrils with respect to isolated peptides in solution, and the effect is significantly stronger for [Tea][Ms]. The secondary structure of fibrils is not much affected, but single peptides in solution show a marked decr<br></div>ease in their $\beta$-strand character, and an increase in <br>$\alpha$-propensity, again especially for [Tea][Ms]. These observations, consistent with the experimental picture, can be traced to two primary effects, i.e., the different ionicity of the [Tea][Ms] and [Tea][H2PO4] water solutions, and the remarkable affinity of peptides for [Ms]^- anions, due to a multiplicity of H-bonds.

scholarly journals Computational Analysis of the Effect of [Tea][Ms] and [Tea][H2PO4] Ionic Liquids on the Structure and Stability of Aβ(17-42) Amyloid Protofibrils

2020 ◽  
Author(s):  
Dorothea Gobbo ◽  
Andrea Cavalli ◽  
Pietro Ballone ◽  
Antonio Benedetto
Keyword(s):  
Free Energy ◽  
Ionic Liquids ◽  
Room Temperature ◽  
Computational Analysis ◽  
Experimental Studies ◽  
Room Temperature Ionic Liquids ◽  
Organic Salts ◽  
Structure And Stability ◽  
Physiological Conditions ◽  
The Stability

<div>Experimental studies have reported the possibility of affecting the growth/dissolution of amyloid fibres by the addition of organic salts of the room-temperature ionic-liquids family, raising the tantalizing prospect of controlling these processes at physiological conditions. The effect of [Tea][Ms] and [Tea][H2PO4] at various concentrations on the structure and stability of a simple model of Aβ42 fibrils has been investigated by computational means. Free energy computations show that both [Tea][Ms] and [Tea][H2PO4] decrease the stability of fibrils with respect to isolated peptides in solution, and the effect is significantly stronger for [Tea][Ms]. The secondary structure of fibrils is not much affected, but single peptides in solution show a marked decr<br></div>ease in their $\beta$-strand character, and an increase in <br>$\alpha$-propensity, again especially for [Tea][Ms]. These observations, consistent with the experimental picture, can be traced to two primary effects, i.e., the different ionicity of the [Tea][Ms] and [Tea][H2PO4] water solutions, and the remarkable affinity of peptides for [Ms]^- anions, due to a multiplicity of H-bonds.

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