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Related Concept Videos

Membrane Domains01:18

Membrane Domains

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.
Protein Domains
The membrane comprises a group of distinct proteins responsible for carrying out a cell's specific function. For example, the plasma membrane of the human sperm, or a single germ cell, contains a unique set of proteins in the anterior...
Fluid Mosaic Model01:19

Fluid Mosaic Model

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 with the analogy of...
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as G-protein-linked receptors (GPCRs) and...
Mechanisms of Membrane Domain Formation00:59

Mechanisms of Membrane Domain Formation

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.
Another mechanism for membrane domain formation involves membrane proteins interacting with cytoskeletal...
Single-pass Transmembrane Proteins01:25

Single-pass Transmembrane Proteins

Integral membrane proteins are tightly associated with the cell membrane and play a crucial role in cell communication, signaling, adhesion, and transport of the molecules. Some integral membrane proteins are present only in the membrane monolayer. For example, the enzyme fatty acid amide hydrolase is present in the cytoplasmic side of the membrane monolayer. In contrast, another type of integral membrane protein, also known as a transmembrane protein, spans across the membrane. Transmembrane...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

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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Related Experiment Video

Updated: May 11, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
07:10

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth

Published on: June 28, 2019

A common landscape for membrane-active peptides.

Nicholas B Last1, Diana E Schlamadinger, Andrew D Miranker

  • 1Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520-8114, USA.

Protein Science : a Publication of the Protein Society
|May 8, 2013
PubMed
Summary

Membrane-active peptides, including antimicrobial, amyloid, and cell-penetrating types, share common physical principles. Their diverse activities arise from a unified energy landscape influencing phospholipid bilayers and membrane defects.

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Last Updated: May 11, 2026

In Vesiculo Synthesis of Peptide Membrane Precursors for Autonomous Vesicle Growth
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Published on: June 28, 2019

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Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis

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Area of Science:

  • Biochemistry
  • Biophysics
  • Molecular Biology

Background:

  • Three main families of membrane-active peptides exist: antimicrobial, amyloid, and cell-penetrating.
  • These peptides are classified by their distinct activities, such as microbial membrane disruption, disease pathology, or cellular translocation.
  • Despite classification differences, similarities in sequence, structure, and activity suggest shared underlying mechanisms.

Purpose of the Study:

  • To propose that diverse membrane-active peptide activities stem from a common set of physical principles.
  • To argue that the observed activities represent different facets of a shared peptide-membrane interaction energy landscape.

Main Methods:

  • Review of existing literature on antimicrobial, amyloid, and cell-penetrating peptides.
  • Analysis of proposed physical principles governing peptide-membrane interactions.
  • Conceptual framework development based on membrane properties, peptide partitioning, and kinetics.

Main Results:

  • Peptides from all three families alter the Brownian properties of phospholipid bilayers.
  • These peptides enhance the sampling of intrinsic membrane fluctuations, including defects.
  • A comprehensive energy landscape can describe peptide interactions with bilayers, considering membrane properties and peptide kinetics.

Conclusions:

  • The activities of antimicrobial, amyloid, and cell-penetrating peptides are unified under a shared energy landscape.
  • Understanding this shared landscape provides a fundamental perspective on membrane-active peptide behavior.
  • This unified view offers insights into peptide-membrane interactions across different biological contexts.