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Institute for Bioengineering and Biosciences
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Lipid Hydroperoxide Compromises the Membrane Structure Organization

Lipid Hydroperoxide Compromises the Membrane Structure Organization | iBB | Scoop.it

Lipid hydroperoxides have recently been recognized as key mediators of diseases (such as neurodegenerative disorders or Type II diabetes) and cell death. In a recent work, structural and dynamic perturbations induced by the hydroperoxidized POPC lipid (POPC-OOH) in fluid POPC membranes were addressed using advanced small-angle X-ray scattering (SAXS) and fluorescence methodologies. Notably, this multidisciplinary approach revealed that the hydroperoxide group located at the membrane interface, promotes a higher membrane hydration and microviscosity, with a strikingly lower order and bending rigidity, an unusual trend in membrane biophysics, which ultimately compromises membrane structure organization. This international work co-led by Ana M. Melo (BSIRG-iBB) and Rosangela Itri (Institute of Physics, University of São Paulo) was recently published in Langmuir and involved other BSIRG-iBB researchers (Ana Coutinho, Alexander Fedorov and Manuel Prieto).

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The Conformational Polymorphism of Disordered Proteins in Neurodegeneration at the Single-molecule Level

The Conformational Polymorphism of Disordered Proteins in Neurodegeneration at the Single-molecule Level | iBB | Scoop.it

Intrinsically disordered proteins/regions (IDPs/IDRs) are widespread in the human proteome and play critical roles in distinct biological processes and dysfunction. Contrary to the classical “structure–function” paradigm, IDPs lack stable secondary/tertiary structures under physiological conditions, and instead adopt a dynamic ensemble of multiple conformations. Moreover, several neurodegenerative disorders are associated with the pathological self-assembly of neuronal IDPs, including tau (Alzheimer’s disease), α-synuclein (Parkinson’s disease), and huntingtin exon 1 (Huntington’s disease). Therefore, there is an emerging medical interest in understanding their physical and structural features. However, their characterization is inherently challenging by traditional ensemble and time-averaging methodologies. A recent review co-authored by Ana Melo from BSIRG-iBB, and published in Frontiers in Molecular Neurosciences the advantages of employing cutting-edge single-molecule fluorescence techniques are discussed to characterize the conformational ensemble of neurodegeneration-promoting IDPs under normal and disease conditions to obtain insights into their gain- or loss-of-function.

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