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Membrane Fluidity01:26

Membrane Fluidity

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Membrane fluidity is explained by the fluid mosaic model of the cell membrane, which describes the plasma membrane structure as a mosaic of components—including phospholipids, cholesterol, proteins, and carbohydrates—that gives the membrane a fluid character.
Mosaic nature of the membrane
The mosaic characteristic of the membrane helps the plasma membrane remain fluid. The integral proteins and lipids exist as separate but loosely-attached molecules in the membrane. The membrane is...
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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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Asymmetric Lipid Bilayer01:35

Asymmetric Lipid Bilayer

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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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Amino acids03:42

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Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...
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Amino acids change solute affinity for lipid bilayers.

Katelyn M Duncan1, William H Steel2, Robert A Walker3

  • 1Department of Chemistry and Biochemistry, Montana State University, Bozeman, Montana.

Biophysical Journal
|July 26, 2021
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Amino acids L-phenylalanine and N-acetyl-DL-tryptophan alter how coumarin molecules interact with lipid membranes. These interactions depend on the amino acid type, coumarin structure, and temperature relative to the lipid phase transition.

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Area of Science:

  • Biophysics
  • Physical Chemistry
  • Materials Science

Background:

  • Lipid bilayers are fundamental to cell membranes.
  • Solute interactions with lipid bilayers are crucial for understanding membrane function and drug delivery.
  • Amino acids can influence membrane properties and solute partitioning.

Purpose of the Study:

  • To investigate the effects of L-phenylalanine (L-PA) and N-acetyl-DL-tryptophan (NAT) on the membrane affinity of coumarin solutes.
  • To explore how temperature and lipid phase transitions affect these interactions.
  • To elucidate the mechanisms by which amino acids modify solute-bilayer interactions.

Main Methods:

  • Time-resolved fluorescence spectroscopy to measure coumarin membrane affinity.
  • Differential scanning calorimetry (DSC) to determine lipid phase transition temperatures.
  • Utilized 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) vesicles as a model membrane system.

Main Results:

  • L-PA increased the partitioning of the tertiary amine coumarin (C152) into the bilayer below the gel-liquid crystalline transition temperature (Tgel-lc).
  • NAT strongly interacted with DPPC bilayers, lowering Tgel-lc and promoting coumarin adsorption to the bilayer surface, with effects diminishing above Tgel-lc.
  • NAT's interaction was primarily surface-adsorbed, unlike L-PA's deeper bilayer penetration.

Conclusions:

  • Amino acids significantly modulate solute affinity for lipid bilayers.
  • The specific effects are dependent on the individual amino acid-lipid-bilayer interactions.
  • Findings suggest implications for understanding protein-lipid interactions and their influence on membrane-associated processes.