HINT predictive analysis of binding between retinol binding protein and hydrophobic ligands.
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.
Marabotti
A
A
Institute of Biochemical Sciences, University of Parma, Italy.
Balestreri
L
L
Cozzini
P
P
Mozzarelli
A
A
Kellogg
G E
GE
Abraham
D J
DJ
D000465:Algorithms; D000970:Antineoplastic Agents / Q000737:chemistry / Q000378:metabolism; D004224:Diterpenes; D017313:Fenretinide / Q000737:chemistry / Q000378:metabolism; D006801:Humans; D008024:Ligands; D008958:Models, Molecular; D011485:Protein Binding; D012177:Retinol-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D012995:Solubility; D014212:Tretinoin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D014801:Vitamin A / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism
D000970:Antineoplastic Agents; D004224:Diterpenes; D008024:Ligands; D012177:Retinol-Binding Proteins; D014801:Vitamin A; D017313:Fenretinide; D014212:Tretinoin; C016250:axerophthene; C054441:retinamide