Characterization of thyroxine-albumin binding using high-performance affinity chromatography II. Comparison of the binding of thyroxine,triiodothyronines and related compounds at the warfarin and indole sites of human serum albumin |
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| Institution: | 1. Atta-ur-Rahman Institute for Natural Product Discovery (AuRIns), Universiti Teknologi MARA Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia;2. Faculty of Applied Science UiTM, 40450 Shah Alam, Selangor, Malaysia;3. Department of Chemistry, COMSATS Institute of Information Technology, Abbottabad 22060, Pakistan;4. Faculty of Pharmacy, Universiti Teknologi MARA Puncak Alam, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia;5. Department of Biosciences, COMSATS Institute of Information Technology, Park Road, Chak Shahzad, Islamabad, Pakistan;6. National Centre of Excellence in Molecular Biology, University of the Punjab, Lahore 53700, Pakistan;7. Department of Chemistry, Hazara University, Mansehra 21120, Pakistan;8. H.E.J. Research Institute of Chemistry, International Center for Chemical and Biological Sciences, University of Karachi, Karachi 75270, Pakistan;1. Atta-ur-Rahman Institute for Natural Product Discovery, Universiti Teknologi MARA (UiTM), Puncak Alam Campus, 42300 Bandar Puncak Alam, Selangor, Malaysia;2. Faculty of Applied Science UiTM, 40450 Shah Alam, Selangor, Malaysia;3. Computational Medicinal Chemistry Laboratory, Department of Biochemistry, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan;4. Department of Chemistry, Hazara University, Mansehra, Khyber Pakhtunkhwa, Pakistan;1. Division of food, medicines and consumer safety, Section Medicinal Products, Scientific Institute of Public Health (WIV-ISP), J. Wytmansstraat 14, B-1050 Brussels, Belgium;2. Department of Toxicology, Dermato-Cosmetology and Pharmacognosy, Center for Pharmaceutical Research (CePhar), Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, B-1090 Brussels, Belgium;1. Department of Chemistry, Hazara University, Mansehra 21300, Khyber Pakhtunkhwa, Pakistan;2. Department of Clinical Pharmacy, Institute for Research and Medical Consultations (IRMC), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia;3. Department of Biochemistry, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan;4. Department of Conservation Sciences, Hazara University, Mansehra 21300, Pakistan;5. Atta-ur-Rahman Institute for Natural Products Discovery (AuRIns), Universiti Teknologi MARA Cawangan Selangor Kampus Puncak Alam, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia;6. Faculty of Pharmacy, Universiti Teknologi MARA Cawangan Selangor Kampus Puncak Alam, 42300 Bandar Puncak Alam, Selangor D. E., Malaysia;7. Chemistry Department, King Fahd University of Petroleum and Minerals, Dhahran 31261, Saudi Arabia;8. Department of Computer Information Systems, College of Computer Science & Information Technology (CCSIT), Imam Abdulrahman Bin Faisal University, P.O. Box 1982, Dammam 31441, Saudi Arabia;1. Natural and Medical Sciences Research Center, University of Nizwa, P.O Box 33, Postal Code 616, Birkat Al Mauz, Nizwa, Oman;2. Department of Biochemistry, Abdul Wali Khan University Mardan, Mardan 23200, Pakistan;3. Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Halle, Germany |
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| Abstract: | High-performance affinity chromatography was used to examine the binding of thyroid hormones and related compounds at the warfarin and indole sites of human serum albumin (HSA). This was studied by continuously applying l-triiodothyronine (l-T3), l-reverse triiodothyronine (l-rT3) or structural analogs of these compounds to an immobilized HSA column while making injections of site-specific probe molecules (i.e. R-warfarin and l-tryptophan). The results were compared with those obtained previously for l-thyroxine (l-T4). Equilibrium association constants and thermodynamic parameters measured by this approach showed good agreement with previous models reported for l-T4 and l-T3 at their high-affinity sites on HSA. This data confirmed that the phenol groups of l-T4 and l-T3 played a significant role in the binding of these compounds at the indole site. Work performed at the warfarin site and with other solutes (e.g. l-rT3) indicated that additional factors, such as interactions through the thyronine backbone or terminal amine and carboxyl groups of these compounds, could also be involved in the binding of thyroid hormones to HSA. |
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