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

Cation-pi interactions involving aromatic amino acids.

Dennis A Dougherty1

  • 1Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125, USA. dadougherty@caltech.edu

The Journal of Nutrition
|May 22, 2007
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

Targeted Mutations Activate Allosteric Modulation of α5-Containing Nicotinic Acetylcholine Receptors.

ACS chemical neuroscience·2026
Same author

Hydrogel Encapsulation of a Designed Fluorescent Protein Biosensor for Continuous Measurements of Sub-100 nM Nicotine.

ACS applied bio materials·2025
Same author

Continuous Nicotine Monitors for Personal Nicotine Pharmacokinetics: A Receptor-Aware Research Agenda.

Nicotine & tobacco research : official journal of the Society for Research on Nicotine and Tobacco·2025
Same author

The Cation-π Interaction in Chemistry and Biology.

Chemical reviews·2025
Same author

Interactive computational and experimental approaches improve the sensitivity of periplasmic binding protein-based nicotine biosensors for measurements in biofluids.

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

β2 nAChR Activation on VTA DA Neurons Is Sufficient for Nicotine Reinforcement in Rats.

eNeuro·2023

Cation-pi interactions, a strong noncovalent force, are vital in nature. Aromatic amino acids like phenylalanine bind cations, influencing protein structure and ligand binding, including neurotransmitters.

Area of Science:

  • Biochemistry
  • Chemical Physics
  • Structural Biology

Background:

  • Cation-pi interactions are fundamental, strong noncovalent forces prevalent in biological systems.
  • Aromatic amino acid side chains (phenylalanine, tyrosine, tryptophan) possess negative electrostatic potential surfaces.
  • These surfaces facilitate binding with various cations via electrostatic interactions.

Purpose of the Study:

  • To provide an overview of the fundamental nature of cation-pi interactions.
  • To illustrate the role of cation-pi interactions in biological contexts, including protein structure and ligand binding.
  • To emphasize the binding of quaternary ammonium ions by aromatic amino acids.

Main Methods:

  • Review of fundamental gas-phase studies characterizing cation-pi interactions.

Related Experiment Videos

  • Analysis of existing literature on cation-pi interactions in proteins.
  • Examination of specific examples involving aromatic amino acids and cations.

    • Main Results:

    • Cation-pi interactions are primarily electrostatic, driven by the negative potential of aromatic amino acid side chains.
    • These interactions contribute significantly to protein secondary structure through associations between aromatic residues and cationic amino acids (lysine, arginine).
    • Cation-pi interactions are crucial for protein-ligand recognition, particularly for binding quaternary ammonium ions like acetylcholine.

    Conclusions:

    • Cation-pi interactions are a versatile and powerful binding force in biological systems.
    • Understanding these interactions is key to comprehending protein structure, function, and molecular recognition.
    • The role of cation-pi interactions in binding small molecules like neurotransmitters highlights their physiological importance.