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Membrane Domains01:18

Membrane Domains

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The membrane domains concentrate specific lipids and proteins at one place within the membrane, which helps in cell signaling, adhesion, and other critical cellular processes. These domains can differ in size, composition, function, and lifespan.
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Different physical properties of lipids and proteins allow them to localize and form distinct islands or domains in the membrane. Some membrane domains are formed due to protein-protein interactions, whereas others are formed due to the presence of specific lipids such as sphingolipids and sterols—for example, large proteins, such as bacteriorhodopsin, aggregate and create distinct domains.
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Microbial membranes exhibit remarkable diversity in lipid composition, reflecting evolutionary adaptations to various environmental conditions. The three domains of life—Bacteria, Archaea, and Eukarya—synthesize membrane lipids through distinct biosynthetic pathways, leading to fundamental structural differences that impact membrane stability, function, and adaptability.Fatty Acid-Based Lipids in Bacteria and EukaryaBacteria and eukaryotes share a common fatty acid biosynthesis...
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Biological membranes show uneven distribution of different types of lipids in the inner and outer layers, resulting in transverse asymmetric membranes. The treatment of the erythrocyte membrane with the enzyme phospholipase confirmed the asymmetric nature of the lipid bilayer. The enzyme hydrolyzes lipids into fatty acids and hydrophilic groups. The phospholipase acts only on the outer layer of the membrane, while the inner layer remains intact. The phospholipase treatment resulted in 80%...
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Scientists identified the plasma membrane in the 1890s and its principal chemical components (lipids and proteins) by 1915. The model for plasma membrane structure, proposed in 1935 by Hugh Davson and James Danielli, was the first model to be widely accepted in the scientific community. The model was based on the plasma membrane's "railroad track" appearance in early electron micrographs. Davson and Danielli theorized that the plasma membrane's structure resembled a sandwich...
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Membrane Fluidity01:23

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Cell membranes are composed of phospholipids, proteins, and carbohydrates loosely attached to one another through chemical interactions. Molecules are generally able to move about in the plane of the membrane, giving the membrane its flexible nature called fluidity. Two other features of the membrane contribute to membrane fluidity: the chemical structure of the phospholipids and the presence of cholesterol in the membrane.
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Author Spotlight: Advancing Cell Membrane Biophysics - Exploring Interactions and Challenges Through Experimental and Computational Approaches
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HsDHODH Microdomain-Membrane Interactions Influenced by the Lipid Composition.

Eduardo F Vicente1, Indra D Sahu2, Edson Crusca3,4

  • 1School of Science and Engineering, São Paulo State University (UNESP) , 17602-496, Tupã, SP Brazil.

The Journal of Physical Chemistry. B
|November 18, 2017
PubMed
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The human dihydroorotate dehydrogenase (HsDHODH) microdomain adopts an alpha-helical structure in membranes, with cardiolipin enhancing its interaction. This flexibility and cardiolipin affinity are key for developing new anti-proliferative disease drugs.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Human dihydroorotate dehydrogenase (HsDHODH) is a target for anti-proliferative disease drug development.
  • The N-terminal microdomain of HsDHODH is crucial for enzyme function, but its dynamics and mechanism are not fully understood.

Purpose of the Study:

  • To investigate the interaction and conformation of the HsDHODH microdomain in model membranes.
  • To understand the role of lipid composition in microdomain structure and function.

Main Methods:

  • Utilized peptide analogues with paramagnetic TOAC at strategic positions.
  • Employed Electron Spin Resonance (ESR) spectroscopy.
  • Studied peptide conformations in buffer, membrane mimetics (micelles), and lipid mixtures (POPC, POPE, cardiolipin).

Main Results:

  • HsDHODH microdomain analogues showed disordered conformations in buffer but adopted significant alpha-helical structures in membrane mimetics.
  • Conformation was lipid-dependent, with enhanced interaction observed in cardiolipin-containing membranes.
  • Observed conformational flexibility in helices, distinct from crystal structures, potentially linked to functional relevance.

Conclusions:

  • The HsDHODH microdomain exhibits significant conformational flexibility and a preferential interaction with cardiolipin-rich membranes.
  • These properties are crucial and should be considered for designing novel HsDHODH inhibitors for proliferative diseases.