Increasing the Resistance of Living Cells against Oxidative Stress by Nonnatural Surfactants as Membrane Guards

The importation of construction principles or even constituents from biology into materials science is a prevailing concept. Vice versa, the cellular level modification of living systems with nonnatural components is much more difficult to achieve. It has been done for analytical purposes, for example, imaging, to learn something about intracellular processes. Cases describing the improvement of a biological function by the integration of a nonnatural (nano)­constituent are extremely rare. Because biological membranes contain some kind of a surfactant, for example, phospholipids, our idea is to modify cells with a newly synthesized surfactant. However, this surfactant is intended to possess an additional functionality, which is the reduction of oxidative stress. We report the synthesis of a surfactant with Janus-type head group architecture, a fullerene C₆₀ modified by five alkyl chains on one side and an average of 20 oxygen species on the other hemisphere. It is demonstrated that the amphiphilic properties of the fullerenol surfactant are similar to that of lipids. Not only quenching of reactive oxygen species (superoxide, hydroxyl radicals, peroxynitrite, and hydrogen peroxide) was successful, but also the fullerenol surfactant exceeds benchmark antioxidant agents such as quercetin. The surfactant was then brought into contact with different cell types, and the viability even of delicate cells such as human liver cells (HepG2) and human dopaminergic neurons (LUHMES) has proven to be extraordinarily high. We could show further that the cells take up the fullerenol surfactant, and as a consequence, they are protected much better against oxidative stress

Locally Resolved Membrane Binding Affinity of the N-Terminus of α-Synuclein

α-Synuclein is abundantly present in Lewy bodies, characteristic of Parkinson’s disease. Its exact physiological role has yet to be determined, but mitochondrial membrane binding is suspected to be a key aspect of its function. Electron paramagnetic resonance spectroscopy in combination with site-directed spin labeling allowed for a locally resolved analysis of the protein–membrane binding affinity for artificial phospholipid membranes, supported by a study of binding to isolated mitochondria. The data reveal that the binding affinity of the N-terminus is nonuniform