Abstract
The structural conformations of phospholipids and cholesterol in phase-separated lipid domains were determined by surface area, transverse density profile, and lipid acyl chain orientational parameter calculations. Binding kinetics and characterization of membrane-bound states of beta-amyloid fibrils of various sizes (dimer to pentamer), on those lipid domains, were determined using protein residue orientational parameter and fibril-residue-lipid minimum distance analysis methods. The energy of binding and characterization of annular lipid shells surrounding the surface-bound amyloid fibrils were also determined. The calculations described above support the article “Coarse-Grained MD simulations Reveal Diverse Membrane-Bound Conformational States of Beta-Amyloid Fibrils in the Liquid-ordered and Liquid-disordered Regions of Phase-Separated Lipid Rafts Containing Glycolipid, Cholesterol and Oxidized Cholesterol (Cheng et al., 2020 [1])”. The reported data is valuable for the future design and analysis of any protein fibrils binding to phase-separated lipid domains in model multi-component lipids membranes using either atomistic or coarse-grained molecular dynamics simulations. Additionally, this data can guide or validate future single-molecule experiments on fibril/membrane interactions in model or cell membranes.
Highlights
The structural conformations of phospholipids and cholesterol in phase-separated lipid domains were determined by surface area, transverse density profile, and lipid acyl chain orientational parameter calculations
The calculations described above support the article “Coarse-Grained MD simulations Reveal Diverse Membrane-Bound Conformational States of BetaAmyloid Fibrils in the Liquid-ordered and Liquid-disordered Regions of Phase-Separated Lipid Rafts Containing Glycolipid, Cholesterol and Oxidized Cholesterol (Cheng et al, 2020 [1])”
The reported data is valuable for the future design and analysis of any protein fibrils binding to phase-separated lipid domains in model multi-component lipids membranes using either atomistic or coarse-grained molecular dynamics simulations
Summary
Modeling and simulations Analysis of lipid conformations and beta-amyloid fibril binding behaviors in phase-separated lipid raft domains, from molecular dynamics simulated data. The data provides useful information about lipid conformations, amyloid-fibril binding behaviours, kinetics, and membrane-bound states, of beta-amyloid fibrils on phase-separated lipid rafts, which mimic the plasma membranes of neurons. The fibril’s membrane-bound orientations, e.g., surface-bound or inserted, and locations in different lipid domains, e.g., glycolipid or cholesterol-enriched (Lo) or -depleted (Ld), or mixed Lod region, will provide insight to guide future experiments to understand the lipid composition and structures on toxic amyloid binding to cell membranes. The simulated data will guide the design of proteins that bind to more complex lipid membranes, containing multiple lipid components and varying domain sizes and structures, that provide a more realistic representation of the complex cell membranes
Sign-in/Register to view highlights & summary Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
