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

Observation of Mechanical and Kinetic Distinctions between Individual Isoleucine and Arginine Residues in a Peptide Dissociating from a Model Lipid Bilayer.

Langmuir : the ACS journal of surfaces and colloids·2026
Same author

Effect of a Negatively Charged Amino Acid Linker on the Tumor-Targeting Properties of [<sup>177</sup>Lu]Lu-Labeled 4‑<i>p</i>‑(Tolyl)butyric Acid-Conjugated Alpha-Melanocyte-Stimulating Hormone Peptides.

ACS pharmacology & translational science·2026
Same author

PS Poly: A chain tracing algorithm to determine persistence length and categorize complex polymers by shape.

PloS one·2026
Same author

Polypyrrole-Coated Microneedle Platform for Offline Electrochemical Detection of Interferon-Alpha in Interstitial Fluid.

ACS applied bio materials·2026
Same author

Matched pair suitability of <sup>89</sup>Zr and <sup>177</sup>Lu-labeled L804-LLP2A theranostics for targeting VLA-4 in melanoma.

Nuclear medicine and biology·2025
Same author

Automated registration and clustering for enhanced localization atomic force microscopy of flexible membrane proteins.

PLoS computational biology·2025

Related Experiment Video

Updated: Mar 5, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
04:45

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

8.0K

Single-Molecule Peptide-Lipid Affinity Assay Reveals Interplay between Solution Structure and Partitioning.

Tina R Matin, Krishna P Sigdel, Milica Utjesanovic

  • 1Department of Chemistry, United States Naval Academy , Annapolis, Maryland 21402, United States.

Langmuir : the ACS Journal of Surfaces and Colloids
|March 28, 2017
PubMed
Summary

Researchers developed a new atomic force microscopy method to measure how protein segments interact with lipid bilayers. This technique distinguishes structural effects on peptide partitioning, advancing our understanding of cellular processes and biotechnology applications.

More Related Videos

Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

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

Published on: July 16, 2020

6.7K
Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

9.4K

Related Experiment Videos

Last Updated: Mar 5, 2026

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions
04:45

Use of Microscale Thermophoresis to Measure Protein-Lipid Interactions

Published on: February 10, 2022

8.0K
Native Cell Membrane Nanoparticles System for Membrane Protein-Protein Interaction Analysis
07:31

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

Published on: July 16, 2020

6.7K
Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry
10:59

Enrichment of Bacterial Lipoproteins and Preparation of N-terminal Lipopeptides for Structural Determination by Mass Spectrometry

Published on: May 21, 2018

9.4K

Area of Science:

  • Biophysics
  • Molecular Biology
  • Biotechnology

Background:

  • Protein-lipid interactions are crucial for cellular functions and have biotechnological relevance.
  • Understanding these interactions is limited by the lack of direct probing methodologies.

Purpose of the Study:

  • To develop and apply a novel single-molecule force spectroscopy assay for probing peptide-lipid bilayer interactions.
  • To investigate the influence of peptide structure and geometry on lipid bilayer partitioning.

Main Methods:

  • Utilized precision atomic force microscopy (AFM)-based single-molecule force spectroscopy.
  • Constructed and tested peptide segments derived from the SecA protein, including variations in geometry.
  • Employed an extended diffusive barrier crossing theory and molecular dynamics simulations for energetic landscape modeling.

Main Results:

  • Successfully distinguished lipid bilayer partitioning interactions for peptides with differing structures.
  • Identified two distinct dissociation pathways for the core SecA2-11 peptide sequence.
  • Observed conformational differences in peptides that correlated with their bilayer partitioning propensity.

Conclusions:

  • The developed AFM methodology provides a powerful tool for dissecting peptide-lipid interactions.
  • Peptide structure significantly impacts its ability to partition into lipid bilayers.
  • This approach is generalizable for studying diverse peptide and lipid systems.