Supported lipid bilayers with incorporated membrane proteins have promising potential for diverse applications, such as filtration processes, drug delivery, and biosensors. For these applications, the continuity (lack of defects), electrical resistivity, and charge capacitance of the lipid bilayers are crucial. Here, we highlight the effects of temperature changes and the rate of temperature changes on the vertical and lateral expansion and contraction of lipid bilayers, which in turn affect the lipid bilayer resistivity and capacitance. We focused on lipid bilayers that consist of 50 mol % dimyristoyl- sn-glycero-3-phosphocholine (zwitterionic lipid) and 50 mol % dimyristoyl-3-trimethylammonium-propane (positively charged lipid) lipids. This lipid mixture is known to self-assemble into a continuous lipid bilayer on silicon wafers. It is shown experimentally and explained theoretically that slow cooling (e.g., -0.4 °C min) increases the resistivity significantly and reduces the capacitance of lipid bilayers, and these trends are reversed by heating. However, fast cooling (∼ -10 °C min or faster) damages the membrane and reduces the resistivity and capacitance of lipid bilayers to practically zero. Importantly, the addition of 50 mol % cholesterol to lipid bilayers prevents the resistivity and capacitance reduction after fast cooling. It is argued that the ratio of lipid diffusion coefficient to thermal expansion/contraction rate (proportional to the heating/cooling rate) is the crucial parameter that determines the effects of temperature changes on lipids bilayers. A high ratio (fast lipid diffusion) increases the lipid bilayer resistivity and decreases the capacitance upon cooling and vice versa. Similar trends are expected for lipid membranes that consist of other lipids or lipidlike mixtures.
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http://dx.doi.org/10.1021/acs.langmuir.9b00726 | DOI Listing |
Langmuir
January 2025
School of Chemical Engineering and Translational Nanobioscience Research Center, Sungkyunkwan University, Suwon 16419, Republic of Korea.
Alkylphospholipids are single-chain lipid amphiphiles that possess clinically relevant biological activities driven by membrane-destabilizing interactions. Subtle variations in alkylphospholipid structure can lead to significant differences in their biological effects, yet corresponding membrane interactions remain underexplored. Herein, we employed the quartz crystal microbalance-dissipation (QCM-D) technique to characterize the real-time membrane interactions of three alkylphospholipids-edelfosine, miltefosine, and perifosine-on supported lipid bilayers with varying cholesterol fractions.
View Article and Find Full Text PDFFEBS Open Bio
January 2025
Institute of Neurophysiology, Charité - Universitätsmedizin Berlin, Corporate Member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Germany.
Neurotransmitter release is triggered in microseconds by the two C domains of the Ca sensor synaptotagmin-1 and by SNARE complexes, which form four-helix bundles that bridge the vesicle and plasma membranes. The synaptotagmin-1 CB domain binds to the SNARE complex via a 'primary interface', but the mechanism that couples Ca-sensing to membrane fusion is unknown. Widespread models postulate that the synaptotagmin-1 Ca-binding loops accelerate membrane fusion by inducing membrane curvature, perturbing lipid bilayers or helping bridge the membranes, but these models do not seem compatible with SNARE binding through the primary interface, which orients the Ca-binding loops away from the fusion site.
View Article and Find Full Text PDFNeuron
January 2025
Department of Neuroscience, Albert Einstein College of Medicine, Bronx, NY 10461, USA. Electronic address:
Neurexin cell-adhesion molecules regulate synapse development and function by recruiting synaptic components. Here, we uncover a mechanism for presynaptic assembly that precedes neurexin recruitment, mediated by interactions between cytosolic proteins and membrane phospholipids. Developmental imaging in C.
View Article and Find Full Text PDFNat Commun
January 2025
Institute for Research in Immunology and Cancer (IRIC), Université de Montréal, Montréal, QC, H3T 1J4, Canada.
Intense research on founding members of the RAS superfamily has defined our understanding of these critical signalling proteins, leading to the premise that small GTPases function as molecular switches dependent on differential nucleotide loading. The closest homologs of H/K/NRAS are the three-member RRAS family, and interest in the MRAS GTPase as a regulator of MAPK activity has recently intensified. We show here that MRAS does not function as a classical switch and is unable to exchange GDP-to-GTP in solution or when tethered to a lipid bilayer.
View Article and Find Full Text PDFJ Chem Theory Comput
January 2025
IBiTech - BioMMedA Group, Ghent University, Corneel Heymanslaan 10, Entrance 98, 9000 Gent, Belgium.
Molecular oxygen (O) is essential for life, and continuous effort has been made to understand its pathways in cellular respiration with all-atom (AA) molecular dynamics (MD) simulations of, e.g., membrane permeation or binding to proteins.
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