Abstract
A computational study of host-guest inclusion complexes between β-cyclodextrin (β-CD) and the 20 natural L-α-aminoacids and some selected pentapeptides was carried out and aimed at understanding the nature of the driving forces and mechanism leading to their formation. Relative complexation energies for the complexes with β-CD were calculated in both cases and the solvation Gibbs free energies were also evaluated for the single L-α-aminoacids. The computed results indicate strong possibilities of formation of inclusion complexes between β-CD and single L-α-aminoacids as well as pentapeptides which have hydrophobic side chains. In addition, noteworthy interactions of the side chain of the pentapeptides with the β-CD were also elucidated. A detailed molecular dynamics calculation of one of the representative pentapeptide/β-CD inclusion complex (β-CD/CH3-Ala-Ala- TYR-Ala-Ala-CH3) in aqueous solution has also been carried out. Molecular dynamics calculations support aspects connected with the formation and description of hydrogen bonds and with the role of dispersion forces in the inclusion complex in water.
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