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

You might also read

Related Articles

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

Sort by
Same author

Molecular regulation and physiological role of GOLPH3-mediated Golgi retention.

Nature communications·2026
Same author

Beyond the Gold Electrode Standard: Using a Triazabutadiene-Maleimide Linker to Covalently Immobilize a Glycan-Polymer Biorecognition Element onto Carbon.

ACS applied bio materials·2026
Same author

Nanodisc-Forming Polymers for the Extraction of Membrane Proteins.

Biomacromolecules·2026
Same author

On the subtleties of cluster construction when defining crystalline nuclei in atomistic simulations.

The Journal of chemical physics·2026
Same author

Core-block engineering enables control of ice recrystallisation inhibition in polymer nanoparticles.

Chemical science·2026
Same author

Modulating the Swelling Behavior of Polymer Brushes via Interfacial Chemistry.

Angewandte Chemie (International ed. in English)·2026

Related Experiment Video

Updated: Nov 6, 2025

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
13:49

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Published on: December 6, 2017

11.6K

A minimalistic cyclic ice-binding peptide from phage display.

Corey A Stevens1, Fabienne Bachtiger2, Xu-Dong Kong3

  • 1Laboratoire des Polymères, Institut des Matériaux and Institut des Sciences et Ingénierie Chimiques, École Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.

Nature Communications
|May 12, 2021
PubMed
Summary
This summary is machine-generated.

Researchers developed a short peptide mimic of ice-binding proteins (IBPs) using phage display. This peptide, essential for ice binding, shows potential for protein purification applications.

More Related Videos

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
07:32

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

7.9K
Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
10:43

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Published on: October 3, 2019

6.0K

Related Experiment Videos

Last Updated: Nov 6, 2025

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates
13:49

Semi-automated Biopanning of Bacterial Display Libraries for Peptide Affinity Reagent Discovery and Analysis of Resulting Isolates

Published on: December 6, 2017

11.6K
Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library
07:32

Screening and Identification of Small Peptides Targeting Fibroblast Growth Factor Receptor2 using a Phage Display Peptide Library

Published on: September 30, 2019

7.9K
Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
10:43

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes

Published on: October 3, 2019

6.0K

Area of Science:

  • Biochemistry
  • Protein Engineering
  • Molecular Biology

Background:

  • Developing synthetic ice-binding proteins (IBPs) is challenging due to limited structure-property relationships.
  • Ice-binding proteins are crucial in various biological processes and have biotechnological applications.

Purpose of the Study:

  • To identify short peptide mimics of ice-binding proteins (IBPs) using phage display.
  • To characterize the ice-binding properties and mechanism of the identified peptide.
  • To demonstrate the biotechnological utility of the peptide for protein purification.

Main Methods:

  • Phage display selection with an ice-affinity protocol.
  • Cyclic peptide identification and synthesis.
  • Mutational analysis to determine essential residues.
  • Molecular dynamics simulations to elucidate binding mechanisms.
  • Protein expression as an 'Ice-Tag' fusion with mCherry.

Main Results:

  • A cyclic 14-amino acid peptide with ice-binding capabilities was identified.
  • Asp8, Thr10, and Thr14 were identified as critical residues for ice binding.
  • Molecular dynamics simulations suggested a hydrophobic binding mechanism involving Thr10.
  • The 'Ice-Tag' fusion protein effectively purified target proteins from cell lysate.

Conclusions:

  • Phage display is a viable method for discovering short peptide mimics of IBPs.
  • The identified peptide exhibits essential ice-binding residues and a potential hydrophobic binding mechanism.
  • The 'Ice-Tag' peptide fusion demonstrates practical potential in biotechnological applications like protein purification.