Serum albumin ligand binding volumes using high pressure denaturation |
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| Institution: | 1. Department of Biothermodynamics and Drug Design, Vilnius University Institute of Biotechnology, V.A. Graičiūno 8, LT-02241 Vilnius, Lithuania;2. Baltic Institute of Advanced Technology, Saulėtekio al. 15, LT-10224 Vilnius, Lithuania;1. Department of Chemistry, Faculty of Science, Jamia Hamdard (Hamdard University), New Delhi 110 062, India;2. Department of Chemistry, University of Delhi, Delhi 110 007, India;1. University of Hohenheim, Institute of Food Science and Biotechnology, Chair of Plant Food Technology and Analysis, Garbenstrasse 25, 70599 Stuttgart, Germany;2. King Abdulaziz University, Faculty of Science, Biological Science Department, P. O. Box 80257, Jeddah 21589, Saudi Arabia;1. Pós-Graduação em Ciência de Materiais, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil;2. Departamento de Bioquímica, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil;3. Departamento de Engenharia Mecânica, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil;4. Departamento de Física, Universidade Federal de Pernambuco, 50670-901 Recife, PE, Brazil;1. Department of Chemistry, Dalian University of Technology, Dalian 116024, Liaoning, China;2. Department of Chemistry, Tsinghua University, Beijing 100084, China;1. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences/Key Laboratory of Agro-Products Processing, Ministry of Agriculture and Rural Affairs, Beijing 100193, China;2. Institute of Food and Nutrition Development, Ministry of Agriculture and Rural Affairs, 12 Zhongguancun South Street, Haidian District, Beijing 100081, China |
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| Abstract: | The pressure shift assay (PSA, also termed either PressureFluor or differential pressure fluorimetry) was used to study the thermodynamics of decanoate and dodecanoate lipid binding to human serum albumin (HSA) in the temperature range from 25 °C to 80 °C and the pressure range from 0.1 MPa to 400 MPa. The ligands stabilized HSA against both pressure and temperature denaturation. The P–T phase diagram for HSA bound to saturated fatty acids is shown. Pressure induced HSA denaturation reversibility is demonstrated via either intrinsic tryptophan or extrinsic probe 1,8-anilinonaphthalene sulfonate (ANS) fluorescence. The effect of guanidinium in a PSA was studied. PSA provides information on ligand binding volumes. The volume changes from protein–ligand binding are thermodynamically important and could be used in designing compounds with specific volumetric binding properties. |
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