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Thermal Reversibility and Disaggregation of Human Serum Albumin Upon Incubation With 3-Β Hydroxybutyrate: A Proposed Mechanism for Thiol Reaction Publisher



Bohlooli M1, 2 ; Moosavimovahedi AA1, 3 ; Taghavi F4 ; Shockravi A5 ; Moosavimovahedi Z6 ; Farhadi M7 ; Saboury AA1, 3 ; Khajeh M2 ; Poursasan N1 ; Goodarzi M1 ; Farivar F1 ; Valipour M1 ; Amanlou M8 ; Sheibani N9 Show All Authors
Authors
  1. Bohlooli M1, 2
  2. Moosavimovahedi AA1, 3
  3. Taghavi F4
  4. Shockravi A5
  5. Moosavimovahedi Z6
  6. Farhadi M7
  7. Saboury AA1, 3
  8. Khajeh M2
  9. Poursasan N1
  10. Goodarzi M1
  11. Farivar F1
  12. Valipour M1
  13. Amanlou M8
  14. Sheibani N9
  15. Habibirezaei M10
Show Affiliations
Authors Affiliations
  1. 1. Institute of Biochemistry and Biophysics (IBB), University of Tehran, Tehran, Iran
  2. 2. Faculty of Science, University of Zabol, Zabol, Iran
  3. 3. Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran
  4. 4. Faculty of Science, Tarbiat Modares University, Tehran, Iran
  5. 5. Department of Chemistry, Kharazmi University, Tehran, Iran
  6. 6. Chemistry and Chemical Engineering Research Center of Iran, Tehran, Iran
  7. 7. ENT-HNS Research Center, IUMS, Tehran, Iran
  8. 8. Department of Medical Chemistry, Faculty of Pharmacy, Tehran University of Medical Sciences, Tehran, Iran
  9. 9. Departments of Ophthalmology and Visual Sciences, University of Wisconsin, School of Medicine and Public Health, Madison, WI, United States
  10. 10. Schools of Biology, University of Tehran, Tehran, Iran

Source: Journal of Thermal Analysis and Calorimetry Published:2015


Abstract

Thermal inactivation of proteins is a main challenge in food technology and medicine. The 3-β-hydroxybutyrate (3BHB) is the most abundant ketone body with a carboxyl group. Its concentration increases during fasting, prolonged exercise, and in diabetic patients. In this work, human serum albumin (HSA) was incubated with 3BHB for 7, 14, 21, and 35 days under physiological conditions. The thermal reversibility and thermal aggregation of HSA upon incubation with 3BHB were determined by differential scanning calorimetry and free amine content assay. These results indicated that 3BHB binds the lysine residues of HSA through nucleophilic attack leading to formation of covalent bonds. The calorimetric results showed that the modification of lysine residues by 3BHB resulted in partial unfolding of HSA compared to the modification of thiol group of Cys34, which is surrounded by other amino acid side chains. Since thermal aggregation of HSA is related to Cys34, its modification caused a decrease in thermal aggregation and an increase in thermal reversibility of modified HSA. © 2014 Akademiai Kiado.