Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

You might also read

Related Articles

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

Sort by
Same author

Sprinkling in extra validation for high-value PTMs and therapeutic Abs with MILKSHAKE Western blots and Sundae ELISAs.

New biotechnology·2025
Same author

Isolation of Peptide Ligands for the HIV Capsid Protein p24 by Phage-Display.

International journal of peptide research and therapeutics·2025
Same author

Engineered FHA domains can bind to a variety of Phosphothreonine-containing peptides.

Protein engineering, design & selection : PEDS·2024
Same author

Correction: Curation of causal interactions mediated by genes associated with autism accelerates the understanding of gene-phenotype relationships underlying neurodevelopmental disorders.

Molecular psychiatry·2024
Same author

Curation of causal interactions mediated by genes associated with autism accelerates the understanding of gene-phenotype relationships underlying neurodevelopmental disorders.

Molecular psychiatry·2023
Same author

Efficient Cloning of Inserts for Phage Display by Golden Gate Assembly.

Methods in molecular biology (Clifton, N.J.)·2023

Related Experiment Video

Updated: Jul 7, 2026

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
08:31

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

Mapping protein-protein interactions with phage-displayed combinatorial peptide libraries.

Brian K Kay1, Luisa Castagnoli

  • 1Argonne National Laboratory, Argonne, Illinois, USA.

Current Protocols in Cell Biology
|January 30, 2008
PubMed
Summary

This study details methods for isolating bacteriophage M13 displaying peptide ligands that bind to specific proteins. These techniques enable the identification of novel protein interactions through consensus sequence analysis.

More Related Videos

A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
12:36

A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits

Published on: February 16, 2014

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Related Experiment Videos

Last Updated: Jul 7, 2026

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions
08:31

Biosensor-based High Throughput Biopanning and Bioinformatics Analysis Strategy for the Global Validation of Drug-protein Interactions

Published on: December 1, 2020

A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits
12:36

A Protocol for Phage Display and Affinity Selection Using Recombinant Protein Baits

Published on: February 16, 2014

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing
12:04

Interactome-Seq: A Protocol for Domainome Library Construction, Validation and Selection by Phage Display and Next Generation Sequencing

Published on: October 3, 2018

Area of Science:

  • Molecular Biology
  • Biotechnology
  • Proteomics

Background:

  • Phage display technology is crucial for identifying protein-ligand interactions.
  • Bacteriophage M13 is a versatile platform for displaying peptide libraries.

Purpose of the Study:

  • To describe methods for affinity selection of bacteriophage M13 displaying combinatorial peptides.
  • To enable the isolation of peptide ligands that bind to specific protein targets.

Main Methods:

  • Affinity selection of bacteriophage M13 from combinatorial peptide libraries.
  • Direct selection using target protein immobilized on microtiter plates.
  • Bead-based affinity selection methods.
  • Enzyme-Linked Immunosorbent Assay (ELISA) for phage purification.

Main Results:

  • Successful isolation of peptide ligands with specific binding affinities to target proteins.
  • Demonstration of both direct and bead-based selection strategies.
  • Identification of consensus sequences from selected phage.

Conclusions:

  • These methods provide a robust approach for discovering novel peptide ligands.
  • The identified peptide ligands and consensus sequences can be used to predict protein interactions.
  • Facilitates the exploration of proteomic databases for putative interacting proteins.