Influence of NaCl on the Structure and Dynamics of Phospholipid Layers

We present a structural and dynamical analysis of the influence of NaCl on multilayer stacks of phospholipids on a solid surface. To this end, multilayer stacks of phospholipids (L-α-phosphatidylcholine, abbreviated as SoyPC) are investigated with neutron reflectometry, grazing-incidence small-angle neutron scattering (GISANS) and grazing-incidence neutron-spin echo spectroscopy (GINSES). We show both that the NaCl influence on the structure is predominantly on water-head group interface and also, that the change in dynamics is restricted to an associated change in the inter-plane viscosity. Using this knowledge, it is possible to model the dynamical behavior of a phospholipid membrane in response to a salt concentration of the solvent using only a single parameter, namely the in-plane viscosity. The excellent agreement with our previously published model also strongly supports the existence of a thermally excited surface mode in phospholipid membranes for close-to-physiological conditions.

Activated nanoscale actin-binding domain motion in the catenin–cadherin complex revealed by neutron spin echo spectroscopy

As the core component of the adherens junction in cell–cell adhesion, the cadherin–catenin complex transduces mechanical tension between neighboring cells. Structural studies have shown that the cadherin–catenin complex exists as an ensemble of flexible conformations, with the actin-binding domain (ABD) of α-catenin adopting a variety of configurations. Here, we have determined the nanoscale protein domain dynamics of the cadherin–catenin complex using neutron spin echo spectroscopy (NSE), selective deuteration, and theoretical physics analyses. NSE reveals that, in the cadherin–catenin complex, the motion of the entire ABD becomes activated on nanosecond to submicrosecond timescales. By contrast, in the α-catenin homodimer, only the smaller disordered C-terminal tail of ABD is moving. Molecular dynamics (MD) simulations also show increased mobility of ABD in the cadherin–catenin complex, compared to the α-catenin homodimer. Biased MD simulations further reveal that the applied external forces promote the transition of ABD in the cadherin–catenin complex from an ensemble of diverse conformational states to specific states that resemble the actin-bound structure. The activated motion and an ensemble of flexible configurations of the mechanosensory ABD suggest the formation of an entropic trap in the cadherin–catenin complex, serving as negative allosteric regulation that impedes the complex from binding to actin under zero force. Mechanical tension facilitates the reduction in dynamics and narrows the conformational ensemble of ABD to specific configurations that are well suited to bind F-actin. Our results provide a protein dynamics and entropic explanation for the observed force-sensitive binding behavior of a mechanosensitive protein complex.

Data Analysis and Background Subtraction in Neutron Spin Echo Spectroscopy

With the constantly improving performance of neutron spin echo (NSE) spectrometers it becomes possible to perform measurements on increasingly complex samples and to study more and more delicate effects. To properly study such effects, proper background correction becomes increasingly important. In this paper, we will review different methods to subtract the buffer from NSE measurements and study the effect of small errors in the subtraction of the background. In the large dynamic range of modern neutron spin-echo spectrometers multiple effects become visible in a single measurement. Specifically, for vesicles both membrane undulations and translational diffusion have an effect on the intermediate scattering function in the NSE time window and here, we will investigate how taking this into account differently affects the results obtained from data analysis.

Understanding near-surface polymer dynamics by a combination of grazing-incidence neutron scattering and virtual experiments

Neutron spin-echo spectroscopy is a unique experimental method for the investigation of polymer dynamics. The combination of neutron spin-echo spectroscopy with grazing-incidence geometry (GINSES) opens the possibility to probe the dynamics of soft-matter materials in the vicinity of the solid substrate in the time range up to 100 ns. However, the usage of the GINSES technique has some peculiarities and, due to the novelty of the method and complexity of the scattering geometry, difficulties in further data analysis occur. The current work discusses how virtual experiments within the distorted-wave Born approximation using the BornAgain software can improve GINSES data treatment and aid the understanding of polymer dynamics in the vicinity of the solid surface. With two examples, poly(N-isopropyl acrylamide) brushes and poly(ethylene glycol) microgels on Si surfaces, the simulation as well as the application of the simulation to the GINSES data analysis are presented. The approach allowed a deeper insight to be gained of the background effect and scattering contribution of different layers.

Surfactant Monolayer Bending Elasticity in Lipase Containing Bicontinuous Microemulsions

Lipase-catalyzed reactions offer many advantages among which a high degree of selectivity combined with the possibility to convert even non-natural substrates are of particular interest. A major drawback in the applicability of lipases in the conversion of synthetically interesting, non-natural substrates is the substantial insolubility of such substrates in water. The conversion of substrates, natural or non-natural, by lipases generally involves the presence of a water–oil interface. In the present paper, we exploit the fact that the presence of lipases, in particular the lipase from Candida antarctica B (CalB), changes the bending elastic properties of a surfactant monolayer in a bicontinuous microemulsion consisting of D2O/NaCl -n-(d)-octane-pentaethylene glycol monodecyl ether (C10E5) in a similar manner as previously observed for amphiphilic block-copolymers. To determine the bending elastic constant, we have used two approaches, small angle neutron scattering (SANS) and neutron spin echo (NSE) spectroscopy. The time-averaged structure from SANS showed a slight decrease in bending elasticity, while on nanosecond time scales as probed with NSE, a stiffening has been observed, which was attributed to adsorption/desorption mechanisms of CalB at the surfactant monolayer. The results allow to derive further information on the influence of CalB on the composition and bending elasticity of the surfactant monolayer itself as well as the underlying adsorption/desorption mechanism.