ArticleThe journal of physical chemistry. B2013
Limited perturbation of a DPPC bilayer by fluorescent lipid probes: a molecular dynamics study.
Article in The journal of physical chemistry. B, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 13 citations in OpenAlex.
- Interaction of Near-Infrared (NIR)-Light Responsive Probes with Lipid Membranes: A Combined Simulation and Experimental Study.Pharmaceutics · 2023Article
- Influence of ceramide on lipid domain stability studied with small-angle neutron scattering: The role of acyl chain length and unsaturation.Chemistry and physics of lipids · 2022Article
- The Secret Lives of Fluorescent Membrane Probes as Revealed by Molecular Dynamics Simulations.Molecules (Basel, Switzerland) · 2020Review
- LipidWrapper: an algorithm for generating large-scale membrane models of arbitrary geometry.PLoS computational biology · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The properties of lipid bilayer nanometer-scale domains could be crucial for understanding cell membranes. Fluorescent probes are often used to study bilayers, yet their effects on host lipids are not well understood. We used molecular dynamics simulations to investigate perturbations in a fluid DPPC bilayer upon incorporation of three indocarbocyanine probes: DiI-C18:0, DiI-C18:2, or DiI-C12:0. We find a 10-12% decrease in chain order for DPPC in the solvation shell nearest the probe but smaller effects in subsequent shells, indicating that the probes significantly alter only their local environment. We also observe order perturbations of lipids directly across from the probe in the opposite leaflet. Additionally, the DPPC headgroup phosphorus-to-nitrogen vector of lipids nearest the probe exhibits preferential orientation pointing away from the DiI. We show that, while DiI probes perturb their local environment, they do not strongly influence the average properties of "nanoscopic" domains containing a few hundred lipids.
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