Acrylamide-hemoglobin adduct: A spectroscopic study
| Autor: | Philip O'Toole, Daniela S. Barreiro, Sofia R. Pauleta, André G. Favinha, Joana Martins |
|---|---|
| Přispěvatelé: | DQ - Departamento de Química, UCIBIO - Applied Molecular Biosciences Unit |
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
Circular dichroism
Visible spectroscopy Acrylamide adduct Heme 02 engineering and technology 010402 general chemistry Photochemistry 01 natural sciences Adduct Analytical Chemistry Hemoglobins symbols.namesake chemistry.chemical_compound Hemoglobin Instrumentation Spectroscopy Acrylamide Circular Dichroism Thermal stability 021001 nanoscience & nanotechnology Blood proteins Atomic and Molecular Physics and Optics 0104 chemical sciences Oxygen Maillard reaction chemistry symbols 0210 nano-technology Oxygen binding |
| Popis: | This work was supported by the Applied Molecular Biosciences Unit – UCIBIO , which is financed by national funds from FCT/MEC ( UIDB/Multi/04378/2020 ). Acrylamide is a neurotoxic and carcinogenic organic compound that is able to bind to several biomolecules and form adducts, through nucleophilic addition and in vivo by the Maillard Reaction, interfering with the biological functions of these molecules. Hemoglobin is one of the most abundant intracellular blood proteins, and thus it is of high interest to understand whether the binding of acrylamide can alter its properties. The interaction of acrylamide with hemoglobin was assessed in a 20:1 ratio, and after a 72 h-incubation period, a decrease of ca. 50% in the absorbance of the hemoglobin's Soret band was observed at 37 °C. This together with the analysis of circular dichroism spectra indicate that acrylamide binds in close proximity to the heme group. These perturbations were confirmed to not correspond to the loss of the heme group and were mostly reverted after passing the protein through a size-exclusion chromatographic matrix, suggesting a dominant non-covalent interaction for the observed effect. The thermodynamic parameters of unfolding in the absence and presence of acrylamide, suggest an interaction based on H-bonds and van der Waals forces that slightly stabilizes hemoglobin. The oxygen binding capacity of hemoglobin does not seem to be hindered, as no differences in the Q bands were observed in the adduct. authorsversion published |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|