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

Ligand Binding and Linkage00:49

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...
Ligand Binding Sites02:40

Ligand Binding Sites

Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
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...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

You might also read

Related Articles

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

Sort by
Same author

Multimodal Physicochemical Characterization of Cross-Linking Activities of Biparatopic Antibodies.

Methods in molecular biology (Clifton, N.J.)·2026
Same author

Elucidating Ligand Charge Effects in MR1 Cell-Surface Translocation Using Molecular Simulations.

Journal of chemical information and modeling·2026
Same author

Gold-Catalyzed Cyclization of Pyrrole-Tethered Allenynes for the Synthesis of 4-Acylindoles and Its Application to the Ergot Alkaloid Scaffold.

Organic letters·2026
Same author

Triplet nitrene-mediated photocatalytic azidation of tertiary C(sp<sup>3</sup>)-H bonds.

Chemical communications (Cambridge, England)·2025
Same author

Design Strategy of Antibody Pairs for Biepitopic Antigen-Templated Chemical Reaction Depending on the Tertiary Structure of the Antigen.

Chemistry (Weinheim an der Bergstrasse, Germany)·2025
Same author

Photoinduced Azidosulfonylative Cyclization of 1,6-Dienes with Sulfonyl Azides.

Chemical & pharmaceutical bulletin·2025

Related Experiment Video

Updated: Jun 26, 2026

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Structure-activity relationship study on polyglutamine binding peptide QBP1.

Kenji Tomita1, H Akiko Popiel, Yoshitaka Nagai

  • 1Graduate School of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8501, Japan.

Bioorganic & Medicinal Chemistry
|January 6, 2009
PubMed
Summary

Polyglutamine binding peptide 1 (QBP1) inhibits toxic protein aggregation in neurodegenerative diseases like Huntington disease. A shorter octapeptide version retains QBP1

More Related Videos

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Related Experiment Videos

Last Updated: Jun 26, 2026

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions
10:26

Biotinylated Cell-penetrating Peptides to Study Intracellular Protein-protein Interactions

Published on: December 20, 2017

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Neuroscience
  • Molecular Biology
  • Biochemistry

Background:

  • Expanded polyglutamine proteins aggregate in the brain, causing neurodegenerative diseases such as Huntington disease.
  • Polyglutamine Binding Peptide 1 (QBP1), an undecapeptide, was previously identified to bind and suppress pathogenic polyglutamine aggregation.
  • Understanding QBP1's structure-activity relationship is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To conduct a structure-activity relationship study of QBP1 to identify key pharmacophores for inhibiting polyglutamine aggregation.
  • To determine the minimum effective structure of QBP1 required for suppressing polyglutamine protein aggregation.

Main Methods:

  • Phage display peptide libraries were used for initial identification of QBP1.
  • Structure-activity relationship studies were performed on QBP1.
  • Truncation studies were conducted to identify the minimal active peptide sequence.

Main Results:

  • A structure-activity relationship study elucidated the pharmacophores responsible for QBP1's inhibitory activity.
  • A truncation study identified an octapeptide as the minimum structure required for suppressing polyglutamine aggregation.
  • The identified octapeptide demonstrated equipotent activity to the full undecapeptide QBP1 in inhibiting aggregation.

Conclusions:

  • The minimal active structure of QBP1 for suppressing polyglutamine aggregation is an octapeptide.
  • This octapeptide is as effective as the parent QBP1, offering a potentially more streamlined therapeutic agent.
  • These findings advance the development of novel therapeutics for polyglutamine-related neurodegenerative diseases.