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Effect of molecular parameters on the binding of phenoxyacetic acid derivatives to albumins |
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| Institution: | 1. Jiangsu Co-Innovation Center of Efficient Processing and Utilization of Forest Resources, College of Chemical Engineering, Nanjing Forestry University, Nanjing 210037, China;2. Suqian Keylab Biochemical Co., Ltd., Suqian, Jiangsu 223800, China;3. The National Academy of Sciences of Ukraine, V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry, 1 Murmanska str., Kyiv 02094, Ukraine;4. Oakwood Chemical, Inc. 730 Columbia Hwy. N, Estill, SC 29918, USA;5. Department of Organic Chemistry I, Faculty of Chemistry, University of the Basque Country UPV/EHU, Paseo Manuel Lardizábal 3, San Sebastián 20018, Spain;6. IKERBASQUE, Basque Foundation for Science, María Díaz de Haro 3, Plaza Bizkaia, Bilbao 48013, Spain |
| Abstract: | The interaction of 12 phenoxyacetic acid derivatives with human and serum albumin as well as with egg albumin was studied by charge-transfer reversed-phase (RP) thin-layer chromatography (TLC) and the relative strength of interaction was calculated. Each phenoxyacetic acid derivative interacted with human and bovine serum albumins whereas no interaction was observed with egg albumin. Stepwise regression analysis proved that the lipophilicity of the derivatives exert a significant impact on their capacity to bind to serum albumins. This result supports the hypothesis that the binding of phenoxyacetic acid derivatives to albumins may involve hydrophobic forces occurring between the corresponding apolar substructures of these derivatives and the amino acid side chains. |
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