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Mechanisms of Membrane-bending01:15

Mechanisms of Membrane-bending

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The living membranes are flexible due to their fluid mosaic nature; however, their bending into different shapes is an active process regulated by specific lipids and proteins. The membrane bending can be transient as seen in vesicles or stable for a long time as in microvilli. Cells regulate the size, location, and duration of the membrane curvature.
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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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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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In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
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Liposome Deformation Induced by Membrane-Binding Peptides.

Kayano Izumi1, Chihiro Saito1, Ryuji Kawano1

  • 1Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, Tokyo 184-8588, Japan.

Micromachines
|February 25, 2023
PubMed
Summary

Cell-penetrating peptides (CPPs) cause greater liposome deformation than antimicrobial peptides (AMPs). Differences in peptide secondary structure influence liposome shape distortion, offering control for molecular robots.

Keywords:
liposome deformationmembrane capacitancepeptide

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Area of Science:

  • Biophysics
  • Materials Science
  • Biochemistry

Background:

  • Liposomes are versatile vesicles with applications in drug delivery and nanotechnology.
  • Peptide-membrane interactions are crucial for understanding biological processes and designing biomimetic systems.
  • Controlling liposome architecture is key for advanced applications like molecular robotics.

Purpose of the Study:

  • To investigate how different membrane-binding peptides affect liposome deformation and shape distortion.
  • To compare the effects of cell-penetrating peptides (CPPs) and antimicrobial peptides (AMPs) on liposome integrity.
  • To explore the potential of using peptide structure to regulate liposome architecture for molecular robotics.

Main Methods:

  • Utilized fluorescent microscopy to monitor liposome deformation.
  • Employed capacitance measurements to estimate peptide binding to lipid bilayers (DOPC membranes).
  • Compared the effects of four peptides: TAT, C105Y (CPPs), melittin, and ovispirin (AMPs).

Main Results:

  • Cell-penetrating peptides (CPPs) induced significantly higher liposome deformation and shape distortion compared to antimicrobial peptides (AMPs).
  • The peptide C105Y did not cause liposome rupture, unlike TAT, melittin, and ovispirin.
  • Observed variations in liposome distortion correlated with peptide secondary structures (α-helix vs. random coil).

Conclusions:

  • Peptide secondary structure plays a critical role in dictating the extent of liposome deformation and distortion.
  • Peptides can be utilized to precisely control liposome architecture.
  • This research provides a foundation for developing peptide-mediated control of liposomal molecular robots.