Preprint Article Version 1 Preserved in Portico This version is not peer-reviewed

Structure and Interdigitation of Chain-Asymmetric Phosphatidylcholines and Milk Sphingomyelin in the Fluid Phase

Version 1 : Received: 30 June 2021 / Approved: 1 July 2021 / Online: 1 July 2021 (22:26:58 CEST)

How to cite: Frewein, M.P.; Doktorova, M.; Heberle, F.A.; Scott, H.L.; Semeraro, E.F.; Porcar, L.; Pabst, G. Structure and Interdigitation of Chain-Asymmetric Phosphatidylcholines and Milk Sphingomyelin in the Fluid Phase. Preprints 2021, 2021070039 (doi: 10.20944/preprints202107.0039.v1). Frewein, M.P.; Doktorova, M.; Heberle, F.A.; Scott, H.L.; Semeraro, E.F.; Porcar, L.; Pabst, G. Structure and Interdigitation of Chain-Asymmetric Phosphatidylcholines and Milk Sphingomyelin in the Fluid Phase. Preprints 2021, 2021070039 (doi: 10.20944/preprints202107.0039.v1).

Abstract

We addressed the frequent occurrence of mixed-chain lipids in biological membranes and their impact on membrane structure by studying several chain-asymmetric phosphatidylcholines and the highly asymmetric milk sphingomyelin. Specifically, we report trans-membrane structures of the corresponding fluid lamellar phases using small-angle X-ray and neutron scattering, which were jointly analyzed in terms of a membrane composition-specific model, including a headgroup hydration shell. Focusing on terminal methyl groups at the bilayer center we found a linear relation between hydrocarbon chain length mismatch and the methyl-overlap for phosphatidylcholines, and a non-negligible impact of the glycerol backbone-tilting, letting the sn1-chain penetrate deeper into the opposing leaflet by half a CH2 group. That is, penetration-depth differences due to the ester-linked hydrocarbons at the glycerol backbone, reported previously for gel phase structures also extend to the physiological more relevant fluid phase, but are significantly reduced. Moreover, milk sphingomyelin was found to follow the same linear relationship suggesting a similar tilt of the sphingosine backbone. Complementary performed molecular dynamics simulations revealed that there is always a part of the lipid tails bending back, even if there is a high interdigitation with the opposing chains. This suggests that hydrocarbon chain interdigitation plays only a minor role in transbilayer coupling. For both cases of adaption to chain length mismatch, chain-asymmetry has a large impact on hydrocarbon chain ordering, inducing disorder in the longer of the two hydrocarbons.

Subject Areas

Mixed-chain lipids; Neutron scattering; X-ray scattering; MD simulations

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