The effect of methanol on the structural parameters of neuronal membrane lipid bilayers.

Korean J Physiol Pharmacol

Department of Dental Pharmacology and Biophysics, School of Dentistry and Research Institute for Oral Biotechnology, Yangsan Campus of Pusan National University, Yangsan 626-870, Korea.

Published: August 2012

AI Article Synopsis

  • The study examined how methanol affects the properties of synaptosomal plasma membrane vesicles (SPMVs) from bovine cerebral cortex, focusing on lipid mobility and protein interactions.
  • Methanol increased the rotational and lateral mobilities of the outer monolayers more significantly than the inner ones and altered the anisotropy of specific phospholipid chains.
  • The findings suggest that methanol enhances lipid fluidity and leads to the clustering of membrane proteins, indicating potential changes in protein dynamics due to its interaction with lipid membranes.

Article Abstract

The structures of the intact synaptosomal plasma membrane vesicles (SPMVs) isolated from bovine cerebral cortexs, and the outer and the inner monolayer separately, were evaluated with 1,6-diphenyl-1,3,5-hexatriene (DPH) and 1,3-di(1-pyrenyl)propane (Py-3-Py) as fluorescent reporters and trinitrophenyl groups as quenching agents. The methanol increased bulk rotational and lateral mobilities of SPMVs lipid bilayers. The methanol increased the rotational and lateral mobilities of the outer monolayers more than of the inner monolayers. n-(9-Anthroyloxy)stearic acid (n-AS) were used to evaluate the effect of the methanol on the rotational mobility at the 16, 12, 9, 6, and 2 position of aliphatic chains present in phospholipids of the SPMVs outer monolayers. The methanol decreased the anisotropy of the 16-(9-anthroyloxy)palmitic acid (16-AP), 12-(9-anthroyloxy)stearic acid (12-AS), 9-(9-anthroyloxy)stearic acid (9-AS), and 6-(9-anthroyloxy)stearic acid (6-AS) in the SPMVs outer monolayer but it increased the anisotropy of 2-(9-anthroyloxy)stearic acid (2-AS) in the monolayers. The magnitude of the increased rotational mobility by the methanol was in the order at the position of 16, 12, 9, and 6 of aliphatic chains in phospholipids of the outer monolayers. Furthermore, the methanol increased annular lipid fluidity and also caused membrane proteins to cluster. The important finding is that was far greater increase by methanol in annular lipid fluidity than increase in lateral and rotational mobilities by the methanol. Methanol alters the stereo or dynamics of the proteins in the lipid bilayers by combining with lipids, especially with the annular lipids. In conclusion, the present data suggest that methanol, in additions to its direct interaction with proteins, concurrently interacts with membrane lipids, fluidizing the membrane, and thus inducing conformational changes of proteins known to be intimately associated with membranes lipids.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3419761PMC
http://dx.doi.org/10.4196/kjpp.2012.16.4.255DOI Listing

Publication Analysis

Top Keywords

lipid bilayers
12
methanol increased
12
outer monolayers
12
methanol
11
rotational lateral
8
lateral mobilities
8
increased rotational
8
rotational mobility
8
position aliphatic
8
aliphatic chains
8

Similar Publications

Structural dynamics of a designed peptide pore under an external electric field.

Biophys Chem

December 2024

Theoretical Molecular Science Laboratory, RIKEN Cluster for Pioneering Research, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan; Computational Biophysics Research Group, RIKEN Center for Computational Science, 7-1-26 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan; Laboratory for Biomolecular Function Simulation, RIKEN Center for Biosystems Dynamics Research, 1-6-5 Minatojima-Minamimachi, Chuo-ku, Kobe, Hyogo 650-0047, Japan.

Membrane potential is essential in biological signaling and homeostasis maintained by voltage-sensitive membrane proteins. Molecular dynamics (MD) simulations incorporating membrane potentials have been extensively used to study the structures and functions of ion channels and protein pores. They can also be beneficial in designing and characterizing artificial ion channels and pores, which will guide further amino acid sequence optimization through comparison between the predicted models and experimental data.

View Article and Find Full Text PDF

B0AT1 (SLC6A19) is a major sodium-coupled neutral amino acid transporter that relies on angiotensin converting enzyme 2 (ACE2) or collectrin for membrane trafficking. Despite its significant role in disorders associated with amino acid metabolism, there is a deficit of comprehensive structure-function understanding of B0AT1 in lipid environment. Herein, we have employed molecular dynamics (MD) simulations to explore the architectural characteristics of B0AT1 in two distinct environments: a simplified POPC bilayer and a complex lipid system replicating the native membrane composition.

View Article and Find Full Text PDF

A FET-based flexible biosensor system for dynamic behavior observation of lipid membrane with nanoparticles .

Lab Chip

January 2025

State Key Laboratory of Precision Measuring Technology and Instruments, School of Precision Instruments and Optoelectronics Engineering, Tianjin University, Tianjin 300072, China.

Nanoparticles have become widely used materials in various fields, yet their mechanism of action at the cellular level after entering the human body remains unclear. Accurately observing the effect of nanosize dimensions on particle internalization and toxicity in cells is crucial, particularly under the conditions of biological activity. With the aim of helping to study the interactions between nanoparticles of varying sizes and active cell membranes, we propose a flexible biosensor system based on a field effect transistor (FET).

View Article and Find Full Text PDF

Photosensitization has a wide range of applications in vastly distant fields. Three key components must be present at the same time to trigger the related photodynamic effect: light, the photosensitizer (PS) and oxygen. Irradiating the sensitizer leads to the formation of reactive oxygen species (ROS).

View Article and Find Full Text PDF

Kingella kingae, an emerging pediatric pathogen, secretes the pore-forming toxin RtxA, which has been implicated in the development of various invasive infections. RtxA is synthesized as a protoxin (proRtxA), which gains its biological activity by fatty acylation of two lysine residues (K558 and K689) by the acyltransferase RtxC. The low acylation level of RtxA at K558 (2-23%) suggests that the complete acylation at K689 is crucial for toxin activity.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!