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 Experiment Videos

Nonclassical hydrophobic effect in membrane binding equilibria.

J Seelig1, P Ganz

  • 1Department of Biophysical Chemistry, Biocenter of the University of Basel, Switzerland.

Biochemistry
|September 24, 1991
PubMed
Summary
This summary is machine-generated.

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

Predicting clinically relevant bleeding in new-onset atrial fibrillation patients initiating oral anticoagulant therapy: External validation of the AF-BLEED score.

Thrombosis research·2025
Same author

Determinants of label non-adherence to non-vitamin K oral anticoagulants in patients with newly diagnosed atrial fibrillation.

European heart journal open·2022
Same author

Effects of short-term increases in personal and ambient pollutant concentrations on pulmonary and cardiovascular function: A panel study analysis of the Multicenter Ozone Study in oldEr subjects (MOSES 2).

Environmental research·2021
Same author

Drug-induced notched T waves.

Netherlands heart journal : monthly journal of the Netherlands Society of Cardiology and the Netherlands Heart Foundation·2021
Same author

Antithrombotic management of patients with atrial fibrillation-Dutch anticoagulant initiatives anno 2020.

Netherlands heart journal : monthly journal of the Netherlands Society of Cardiology and the Netherlands Heart Foundation·2020
Same author

Changes in anticoagulant prescription in Dutch patients with recent-onset atrial fibrillation: observations from the GARFIELD-AF registry.

Thrombosis journal·2020
Same journal

Aromatic Cage-Directed Azide-Methyllysine Photochemistry for Profiling Nonhistone Interacting Partners of the MeCP2 Methyl-CpG-Binding Domain.

Biochemistry·2026
Same journal

Differential Hydroxypyruvate Processing by <i>E. coli</i> and <i>P. aeruginosa</i> DXP Synthases Reveals Preferential Xylulose 5-Phosphate Formation by the <i>P. aeruginosa</i> Enzyme.

Biochemistry·2026
Same journal

Structural and Functional Characterization of Heterologous Nitrogenase Complexes.

Biochemistry·2026
Same journal

Discovery of Bacterial Unspecific Peroxygenases.

Biochemistry·2026
Same journal

Lactate Biology: Subcellular Routing and Chemical Form Define Function.

Biochemistry·2026
Same journal

Nature's Anaerobic Toolkit: Glycyl Radical Enzymes and Their Expanding Functional and Mechanistic Diversity.

Biochemistry·2026
See all related articles

This study used titration calorimetry to measure the enthalpy of transfer for four amphiphilic molecules into lipid membranes. Enthalpy, not entropy, drives the binding of most of these molecules to the membrane.

Area of Science:

  • Biophysical Chemistry
  • Membrane Biophysics
  • Thermodynamics

Background:

  • Amphiphilic molecules interact with lipid membranes, influencing membrane properties.
  • Understanding these interactions is crucial for drug delivery and membrane function.
  • Previous studies suggest hydrophobic effects primarily drive membrane partitioning.

Purpose of the Study:

  • To quantify the enthalpy of transfer for charged amphiphiles from aqueous to lipid phases.
  • To elucidate the thermodynamic driving forces behind amphiphile-membrane binding.
  • To compare enthalpy-driven vs. entropy-driven processes in membrane interactions.

Main Methods:

  • Titration calorimetry was employed to measure heat changes.
  • Four amphiphilic molecules were studied: TNS, TPB, amlodipine, and dibucaine.

Related Experiment Videos

  • Binding to 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine vesicles was analyzed.

    • Main Results:

    • All four molecules transferred to the hydrophobic membrane core.
    • Binding constants ranged from 600 M-1 (dibucaine) to 60,000 M-1 (TPB).
    • Enthalpies of transfer (-9 kcal/mol for TNS, TPB, amlodipine) largely accounted for free energy changes, indicating enthalpy-driven binding.

    Conclusions:

    • The binding of TNS, TPB, and amlodipine to lipid membranes is primarily enthalpy-driven.
    • This contrasts with the classical entropy-driven hydrophobic effect.
    • Dibucaine binding was less enthalpy-driven but still significant, with temperature-dependent enthalpies observed.