Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Ligand Binding Sites

Ligand Binding Sites

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.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...

Lipids as Anchors

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Mitigating Excessive Mitochondrial Fission Through the Development of a Selective Macrocyclic Inhibitor Targeting Fis1/Mid51 Signaling.

Journal of medicinal chemistry·2026

Same author

Nanoclusters of small amphiphilic molecules in a raft-mimicking model membrane.

Biochimica et biophysica acta. Biomembranes·2026

Same author

Clustering of Spin-Labeled Molecules in Membranes: What Information Can Be Obtained From Electron-Electron Double Resonance.

Journal of peptide science : an official publication of the European Peptide Society·2026

Same author

Fast fourteen-frequency impedance spectroscopy of single erythrocytes and yeast cells in flow.

Biosensors & bioelectronics·2026

Same author

Tailoring NiO-Based Nanostructures for the Electrochemical Valorization of Ethanol: Structure-Property Insights.

Nanomaterials (Basel, Switzerland)·2026

Same author

C-Terminal Nucleobase Modification Amplifies Peptide-Mediated Liposome Fusion.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026

Search research articles

Related Experiment Video

Updated: Sep 21, 2025

Peptide-based Identification of Functional Motifs and their Binding Partners

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Peptide-membrane binding is not enough to explain bioactivity: A case study.

Victoria N Syryamina¹, Ekaterina F Afanasyeva¹, Sergei A Dzuba²

¹Voevodsky Institute of Chemical Kinetics and Combustion, RAS, Novosibirsk 630090, Russian Federation.

Biochimica Et Biophysica Acta. Biomembranes

|June 6, 2022

Summary

This summary is machine-generated.

Antimicrobial peptides

Keywords:

Bioactivity EPR/ESR Lateral lipid organization Membrane-active peptides Trichogin

More Related Videos

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Related Experiment Videos

Last Updated: Sep 21, 2025

Peptide-based Identification of Functional Motifs and their Binding Partners

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Fluorescent Leakage Assay to Investigate Membrane Destabilization by Cell-Penetrating Peptide

Published on: December 19, 2020

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Area of Science:

Biophysics
Membrane Biology
Medicinal Chemistry

Background:

Membrane-active peptides show potential as antimicrobial and anticancer drugs.
Understanding their molecular mechanisms is key to therapeutic development.

Purpose of the Study:

Investigate the membrane interactions of two trichogin GA IV peptide analogs with differing bioactivity.
Determine the molecular basis for selective cancer cell killing versus complete non-toxicity.

Main Methods:

Utilized Electron Paramagnetic Resonance (EPR) spectroscopy.
Studied peptide interaction with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) model membranes.
Analyzed peptide localization, oligomerization, and impact on lipid organization.

Main Results:

Both analogs (Tri(Api^8) and Tri(Leu^4)) bind to membranes and show weak oligomerization.
Neither analog significantly altered lipid membrane organization.
The parent trichogin peptide, unlike the analogs, dimerizes readily and reorganizes membranes.

Conclusions:

Peptide oligomerization and molecular motion, not just membrane binding, are critical for trichogin's bioactivity.
Subtle sequence modifications affecting oligomerization or motion can tune peptide activity.
This provides a basis for designing targeted membrane-active therapeutics.