Spectral features in isolated neutron stars induced by inhomogeneous surface temperatures

The thermal X-ray spectra of several isolated neutron stars display deviations from a pure blackbody. The accurate physical interpretation of these spectral features bears profound implications for our understanding of the atmospheric composition, magnetic field strength and topology, and equation of state of dense matter. With specific details varying from source to source, common explanations for the features have ranged from atomic transitions in the magnetized atmospheres or condensed surface, to cyclotron lines generated in a hot ionized layer near the surface. Here, we quantitatively evaluate the X-ray spectral distortions induced by inhomogeneous temperature distributions of the neutron star surface. To this aim, we explore several surface temperature distributions, we simulate their corresponding general relativistic X-ray spectra (assuming an isotropic, blackbody emission), and fit the latter with a single blackbody model. We find that, in some cases, the presence of a spurious ‘spectral line’ is required at a high significance level in order to obtain statistically acceptable fits, with central energy and equivalent width similar to the values typically observed. We also perform a fit to a specific object, RX J0806.4−4123, finding several surface temperature distributions able to model the observed spectrum. The explored effect is unlikely to work in all sources with detected lines, but in some cases it can indeed be responsible for the appearance of such lines. Our results enforce the idea that surface temperature anisotropy can be an important factor that should be considered and explored also in combination with more sophisticated emission models like atmospheres.

Muscle-Type Nicotinic Receptor Blockade by Diethylamine, the Hydrophilic Moiety of Lidocaine

Lidocaine bears in its structure both an aromatic ring and a terminal amine, which can be protonated at physiological pH, linked by an amide group. Since lidocaine causes multiple inhibitory actions on nicotinic acetylcholine receptors (nAChRs), this work was aimed to determine the inhibitory effects of diethylamine (DEA), a small molecule resembling the hydrophilic moiety of lidocaine, on Torpedo marmorata nAChRs microtransplanted to Xenopus oocytes. Similarly to lidocaine, DEA reversibly blocked acetylcholine-elicited currents (IACh) in a dose-dependent manner (IC50 close to 70 μM), but unlike lidocaine, DEA did not affect IACh desensitization. IACh inhibition by DEA was more pronounced at negative potentials, suggesting an open-channel blockade of nAChRs, although roughly 30% inhibition persisted at positive potentials, indicating additional binding sites outside the pore. DEA block of nAChRs in the resting state (closed channel) was confirmed by the enhanced IACh inhibition when pre-applying DEA before its co-application with ACh, as compared with solely DEA and ACh co-application. Virtual docking assays provide a plausible explanation to the experimental observations in terms of the involvement of different sets of drug binding sites. So, at the nAChR transmembrane (TM) domain, DEA and lidocaine shared binding sites within the channel pore, giving support to their open-channel blockade; besides, lidocaine, but not DEA, interacted with residues at cavities among the M1, M2, M3, and M4 segments of each subunit and also at intersubunit crevices. At the extracellular (EC) domain, DEA and lidocaine binding sites were broadly distributed, which aids to explain the closed channel blockade observed. Interestingly, some DEA clusters were located at the α-γ interphase of the EC domain, in a cavity near the orthosteric binding site pocket; by contrast, lidocaine contacted with all α-subunit loops conforming the ACh binding site, both in α-γ and α-δ and interphases, likely because of its larger size. Together, these results indicate that DEA mimics some, but not all, inhibitory actions of lidocaine on nAChRs and that even this small polar molecule acts by different mechanisms on this receptor. The presented results contribute to a better understanding of the structural determinants of nAChR modulation.