Abstract
The interaction between the retinol binding protein and four ligands was evaluated using HINT, a software based on experimental LogP values of individual atoms. A satisfactory correlation was found between the HINT scores and the experimental dissociation constants of three of the ligands, fenretinide, N-ethylretinamide and all-trans retinol, despite their hydrophobic nature. A prediction is made for the binding affinity of the fourth ligand, axerophtene, not yet determined in solution.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Algorithms
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Antineoplastic Agents / chemistry
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Antineoplastic Agents / metabolism
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Diterpenes
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Fenretinide / chemistry
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Fenretinide / metabolism
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Humans
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Ligands
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Models, Molecular
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Protein Binding
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Retinol-Binding Proteins / chemistry
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Retinol-Binding Proteins / metabolism*
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Solubility
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Tretinoin / analogs & derivatives*
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Tretinoin / chemistry
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Tretinoin / metabolism
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Vitamin A / analogs & derivatives*
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Vitamin A / chemistry
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Vitamin A / metabolism
Substances
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Antineoplastic Agents
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Diterpenes
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Ligands
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Retinol-Binding Proteins
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Vitamin A
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Fenretinide
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Tretinoin
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axerophthene
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retinamide