Investigating hydrogen peroxide induced damage to alpha-2-macroglobulin: Biophysical and thermodynamic study (Englisch)

In: Journal of Molecular Structure ;  1195 ;  904-913 ;  2019
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Abstract Hydrogen peroxide (H2O2) is an important signalling molecule and a non-radical reactive oxygen species (ROS) which can convert into more potent oxygen radicals leading to oxidative stress. The correlation between oxidative stress and the cellular proteinase-antiproteinase balance has been a major component in the development of several pathologies such as emphysema and cystic fibrosis. The present studies attempt to explore the functional inactivation and structural alterations induced in one of the major antiproteinase, alpha-2-macroglobulin (α2M) on interaction with H2O2. α2M, purified from sheep blood plasma is a highly abundant proteinase inhibitor which acts as a backup or reserve force of antiproteinase. Our studies provide biophysical insights into the interaction of H2O2 with sheep α2M. Result demonstrates that antiproteolytic activity of α2M was significantly lowered upon interaction with increasing concentration of H2O2. Analysis of fluorescence spectra reveals quenching of fluorescence intensity in a static manner which occurs due to ground state complex formation. Synchronous fluorescence illustrates alteration in microenvironment around tryptophan and tyrosine residues of α2M. Additionally, UV/visible spectroscopy, circular dichroism and fourier transform infrared spectroscopy results confirms the alteration in secondary structure and conformation of α2M due to H2O2 induced modification. Moreover, polyacrylamide gel electrophoresis also confirms the structural change in α2M on H2O2 interaction. Thermodynamic parameters of H2O2 binding with α2M obtained by ITC indicate the reaction to be exothermic and spontaneous. Our studies suggest that H2O2 induces functional inactivation and structural disruption of sheep α2M possibly due to perturbation of secondary structure, at concentration of oxidant achievable in patho-physiological conditions such as cancer.

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Highlights Increased H2O2 concentration decreases the antiproteinase activity of α2M significantly. Spectroscopic and thermodynamic studies support alteration in secondary structure and conformation of α2M. ITC reveals the binding to be exothermic and spontaneous. Present work signifies H2O2 is a potent inactivator of α2M at concentration achievable in patho-physiological conditions.

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