Dataset Information

Distance tuneable integral membrane protein containing floating bilayers via in situ directed self-assembly.

ABSTRACT: Model membranes allow for structural and biophysical studies on membrane biochemistry at the molecular level, albeit on systems of reduced complexity which can limit biological accuracy. Floating supported bilayers offer a means of producing planar lipid membrane models not adhered to a surface, which allows for improved accuracy compared to other model membranes. Here we communicate the incorporation of an integral membrane protein complex, the multidomain β-barrel assembly machinery (Bam), into our recently developed in situ self-assembled floating supported bilayers. Using neutron reflectometry and quartz crystal microbalance measurements we show this sample system can be fabricated using a two-step self-assembly process. We then demonstrate the complexity of the model membrane and tuneability of the membrane-to-surface distance using changes in the salt concentration of the bulk solution. Results demonstrate an easily fabricated, biologically accurate and tuneable membrane assay system which can be utilized for studies on integral membrane proteins within their native lipid matrix.

SUBMITTER: Hall SCL

PROVIDER: S-EPMC11256219 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature

ACCESS DATA

Publications

Distance tuneable integral membrane protein containing floating bilayers <i>via in situ</i> directed self-assembly.

Hall Stephen C L SCL Hardy David J DJ Bragginton Éilís C ÉC Johnston Hannah H Onose Tudor T Holyfield Rachel R Sridhar Pooja P Knowles Timothy J TJ Clifton Luke A LA

Nanoscale 20240718 28

Model membranes allow for structural and biophysical studies on membrane biochemistry at the molecular level, albeit on systems of reduced complexity which can limit biological accuracy. Floating supported bilayers offer a means of producing planar lipid membrane models not adhered to a surface, which allows for improved accuracy compared to other model membranes. Here we communicate the incorporation of an integral membrane protein complex, the multidomain β-barrel assembly machinery (Bam), int ...[more]

PMID: 38940744

Similar Datasets

Project description:In recent years, many efforts have been devoted to investigating the interaction of nanoparticles (NPs) with lipid biomimetic interfaces, both from a fundamental perspective aimed at understanding relevant phenomena occurring at the nanobio interface and from an application standpoint for the design of novel lipid-nanoparticle hybrid materials. In this area, recent reports have revealed that citrate-capped gold nanoparticles (AuNPs) spontaneously associate with synthetic phospholipid liposomes and, in some cases, self-assemble on the lipid bilayer. However, the mechanistic and kinetic aspects of this phenomenon are not yet completely understood. In this study, we address the kinetics of interaction of citrate-capped AuNP with lipid vesicles of different rigidities (gel-phase rigid membranes on one side and liquid-crystalline-phase soft membranes on the other). The formation of AuNP-lipid vesicle hybrids was monitored over different time and length scales, combining experiments and simulation. The very first AuNP-membrane contact was addressed through molecular dynamics simulations, while the structure, morphology, and physicochemical features of the final colloidal objects were studied through UV-visible spectroscopy, small-angle X-ray scattering, dynamic light scattering, and cryogenic electron microscopy. Our results highlight that the physical state of the membrane triggers a series of events at the colloidal length scale, which regulate the final morphology of the AuNP-lipid vesicle adducts. For lipid vesicles with soft membranes, the hybrids appear as single vesicles decorated by AuNPs, while more rigid membranes lead to flocculation with AuNPs acting as bridges between vesicles. Overall, these results contribute to a mechanistic understanding of the adhesion or self-assembly of AuNPs onto biomimetic membranes, which is relevant for phenomena occurring at the nano-bio interfaces and provide design principles to control the morphology of lipid vesicle-inorganic NP hybrid systems.

Dataset Information

Distance tuneable integral membrane protein containing floating bilayers via in situ directed self-assembly.

Publications

Distance tuneable integral membrane protein containing floating bilayers <i>via in situ</i> directed self-assembly.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets