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Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: evidence from partition coefficients and molecular dynamics simulations.
Journal article

Solvent-dependent conformation and hydrogen-bonding capacity of cyclosporin A: evidence from partition coefficients and molecular dynamics simulations.

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  • 1993-11-26
Published in:
  • Journal of medicinal chemistry. - 1993
Amino Acid Isomerases
Carbon Tetrachloride
Carrier Proteins
Chemical Phenomena
Chemistry, Physical
Chromatography
Computer Simulation
Crystallography, X-Ray
Cyclosporine
Heptanes
Hydrogen Bonding
Models, Molecular
Octanols
Peptidylprolyl Isomerase
Protein Conformation
Solvents
English The partition coefficient of cyclosporin A (CsA) was measured in octanol/water and heptane/water by centrifugal partition chromatography. By comparison with results from model compounds, it was deduced that the hydrogen-bonding capacity of CsA changed dramatically from an apolar solvent (where it is internally H-bonded) to polar solvents (where it exposes its H-bonding groups to the solvent). Molecular dynamics simulations in water and CCl4 support the suggestion that CsA undergoes a solvent-dependent conformational changes and that the interconversion process is slow on the molecular dynamics time scale.
Language
  • English
Open access status
closed
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Persistent URL
https://sonar.rero.ch/global/documents/282884
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