1. The Binding of Synthetic Retinoids to Lipocalin β-Lactoglobulins
- Author
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Jari Yli-Kauhaluoma, Mikko J. Vainio, Mikko Vahermo, Pia Vuorela, Leena Pohjala, Jonna Heikura, Laura H. Riihimäki-Lampén, Vesa Virtanen, and Kaija H. Valkonen
- Subjects
Models, Molecular ,medicine.drug_class ,Biological Availability ,Carboxamide ,Lactoglobulins ,Lipocalin ,Crystallography, X-Ray ,01 natural sciences ,Retinoids ,Structure-Activity Relationship ,03 medical and health sciences ,Drug Discovery ,medicine ,Animals ,Retinoid ,030304 developmental biology ,chemistry.chemical_classification ,0303 health sciences ,Binding Sites ,Molecular Structure ,010405 organic chemistry ,Chemistry ,food and beverages ,Biological activity ,Hydrogen-Ion Concentration ,Lipocalins ,In vitro ,0104 chemical sciences ,3. Good health ,Ultrafiltration (renal) ,Biochemistry ,Drug Design ,Molecular Medicine ,Cattle ,Glycoprotein ,Reindeer - Abstract
The binding of therapeutically relevant synthetic retinoid derivatives to bovine and reindeer beta-lactoglobulin (betaLG) is demonstrated using fluorescence quenching and ultrafiltration/HPLC methods. Furthermore, synthesis of methyl (E)-3-[4-[(E)-2-(2,6,6-trimethylcyclohex-1-enyl)vinyl]phenyl]-acrylate 4 and (E)-3-[4-[(E)-2-(2,6,6-trimethylcyclohex-1-enyl)vinyl]phenyl]acrylic acid 5 is described. All studied compounds bind to both betaLG homologues with nanomolar K(d) values, and the interaction diminishes the pH-dependent aggregation of retinoids. Thus, betaLG may show benefits in improving the bioavailability of retinoid derivatives.
- Published
- 2009
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