Detail study on the interaction between perfluorooctanoic acid (PFOA) with human hemoglobin (Hb)
N.L. Dilani Perera, J. Fuentes Betancourt, Jaroslava Mikšovská, Kevin Ε. Ο'Shea
Abstract
M. PFOA binding at low concentrations occurs at the high-affinity sites leading to the destabilization of the protein structure as reflected by changes in the CD spectrum. PFOA interactions with Hb also interfere with the kinetics of CO association to this protein. The rate for CO association to Hb increases at low PFOA concentrations, whereas at elevated PFOA concentrations, the ligand association is biphasic as a new kinetic process with a different rate constant was observed. Overall, this study provides a detailed explanation of PFOA-induced structural and conformational changes to the Hb protein based on the spectroscopy data.
Topics & Concepts
ChemistryPerfluorooctanoic acidHemoglobinCircular dichroismDissociation constantAbsorbanceEquilibrium constantFerricTitrationBinding siteBiochemistryInorganic chemistryChromatographyReceptorPer- and polyfluoroalkyl substances researchQuantum Electrodynamics and Casimir EffectHeme Oxygenase-1 and Carbon Monoxide