A critical approach to the thermodynamic characterization of inclusion complexes: multiple-temperature isothermal titration calorimetric studies of native cyclodextrins with sodium dodecyl sulfate.

Inclusion complexes based on native cyclodextrins are basic building blocks for the design of a new generation of promising materials. The design process can be optimized by maximizing the population of the desired chemical species. This is greatly facilitated by an accurate characterization of the thermodynamic parameters for their formation. A critically assessed literature review of equilibrium constants for cyclodextrin:sodium dodecyl sulfate (CD:SDS) complexes is reported. We performed multiple-temperature isothermal titration calorimetric (283-323 K) measurements for these systems, leading to the first reported heat capacity changes of binding. Data were analyzed using two thermodynamic models by homemade programs that also provide the distribution of chemical species as a function of the experimental variables. Assisted by earlier molecular dynamic simulations, a microscopic-level discussion of the contributions to the thermodynamic parameters is given. On the basis of our results, a number of recommendations to obtain reliable association parameters for CD-based inclusion complexes are listed.

Similarities and differences between cyclodextrin-sodium dodecyl sulfate host-guest complexes of different stoichiometries: molecular dynamics simulations at several temperatures.

An extensive dynamic and structural characterization of the supramolecular complexes that can be formed by mixing α-, ß-, and γ-cyclodextrin (CD) with sodium dodecyl sulfate (SDS) in water at 283, 298, and 323 K was performed by means of computational molecular dynamics simulations. For each CD at the three temperatures, seven different initial conformations were used, generating a total of 63 trajectories. The observed stoichiometries, intermolecular distances, and relative orientation of the individual molecules in the complexes, as well as the most important interactions which contribute to their stability and the role of the solvent water molecules were studied in detail, revealing clear differences and similarities between the three CDs. Earlier reported findings in the inclusion complexes field are also discussed in the context of the present results. For any of the three native cyclodextrins, the CD(2)SDS(1) species in the head-to-head conformation appears to be a promising building block for nanotubular aggregates both in the bulk and at the solution/air interface, as earlier suggested for the case of α-CD. Moreover, the observed noninclusion arrangements involving ß-CD are proposed as the seed for the premicellar (ß-CD)-induced aggregation of SDS described in the literature.

Molecular dynamics study of triosephosphate isomerase from Trypanosoma cruzi in water/decane mixtures.

A comprehensive study of the triosephosphate isomerase from the parasite Trypanosoma cruzi (TcTIM) in water, in decane, and in three water/decane mixtures was performed using molecular dynamics (MD) simulations in a time scale of 40 ns. The structure and dynamics of the enzyme, as well as the solvent molecules' distribution and mobility, were analyzed in detail. In the presence of decane, the amplitudes of the most important internal motions of the enzyme backbone were observed to depend on the solvent concentration: the higher the water concentration, the greater the amplitudes. Contrary to this trend, the amplitudes of the TcTIM motions in pure water were similar to those of the simulation with the lowest water concentration. The enzyme was observed to be almost motionless in pure decane due to a sharp increase of the number of intramolecular hydrogen bonds. This caused a contraction of the enzyme structure accompanied by a loss of secondary structure and of a decrease of the hydrophilic solvent accessible surface. A similar behavior, although to a lesser extent, was observed in the simulation at the lowest water concentration. Our results suggest that the presence of decane molecules located at specific sites of the enzyme might accelerate its internal movements, although a minimum number of water molecules is needed for the protein to keep its structure and dynamics. Altogether, this work provides new insight into protein and water behavior in organic solvents as well as into the dynamics of TcTIM itself.

Cyclodextrin-based self-assembled nanotubes at the water/air interface.

Native alpha-cyclodextrin (alpha-CD) is found to spontaneously form films at aqueous solution/air interfaces. Shape-response measurements to volume perturbations on drops hanging from a capillary indicate that temperature and sodium dodecyl sulfate (SDS) concentration strongly modify the viscoelastic properties of such films. By using isothermal titration calorimetry (ITC), Brewster angle microscopy (BAM), atomic force microscopy (AFM), and molecular dynamics (MD) simulations, it is shown that the films consist of self-assembled nanotubes whose building blocks are cyclodextrin dimers (alpha-CD2) and alpha-CD2-SDS1 complexes.