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

Protein Folding01:25

Protein Folding

7.9K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
7.9K
The Proteasome01:13

The Proteasome

827
Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
827
Amyloid Fibrils03:03

Amyloid Fibrils

9.5K
Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining,...
9.5K
Protein-protein Interfaces02:04

Protein-protein Interfaces

12.5K
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...
12.5K

You might also read

Related Articles

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

Sort by
Same author

External Acoustic Meatus Approach for Ultrasonographic Evaluation of the Temporomandibular Joint: An Anatomical Validation and Proof-of-Concept Study.

Clinical anatomy (New York, N.Y.)·2026
Same author

Investigating Intraspecific Attacks in Brown Bears (<i>Ursus arctos</i>) Using a Forensic Approach: Evidence from Northern Italy.

Animals : an open access journal from MDPI·2026
Same author

Effects of Human Recombinant Growth Hormone (rhGH) Treatment on Plasma Extracellular Vesicles in GH-Deficient Children: A Preliminary Report.

Journal of clinical medicine·2026
Same author

Combination of hypoxia and hyperosmolarity reduces <i>in vitro</i> chondrocyte de-differentiation.

Frontiers in veterinary science·2026
Same author

Telomere shortening in workers occupationally exposed to a wide range of mostly low benzene levels: a multicenter study.

Scientific reports·2026
Same author

Genetic diversity and circulation of influenza A viruses in Italian pig farms: insights from surveillance and vaccination.

Porcine health management·2026

Related Experiment Video

Updated: Jun 21, 2025

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

11.8K

A Peptide Strategy for Inhibiting Different Protein Aggregation Pathways.

Tommaso Garfagnini1, Luca Ferrari2,3,4, Margreet B Koopman2,3

  • 1Institute of Chemistry, The Hebrew University of Jerusalem, Edmond J. Safra Campus at Givat Ram, 9190401, Jerusalem, Israel.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|July 7, 2024
PubMed
Summary

Researchers developed novel peptides that inhibit protein aggregation, a key factor in many diseases. These multi-targeting compounds show promise for developing new treatments against diverse protein aggregation disorders.

Keywords:
Amyloid fibrilsPeptide arraysPeptide designProtein aggregation inhibitionTau

More Related Videos

Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

12.4K
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

11.3K

Related Experiment Videos

Last Updated: Jun 21, 2025

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
08:48

Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation

Published on: January 26, 2016

11.8K
Peptide-based Identification of Functional Motifs and their Binding Partners
14:28

Peptide-based Identification of Functional Motifs and their Binding Partners

Published on: June 30, 2013

12.4K
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

11.3K

Area of Science:

  • Biochemistry and Molecular Biology
  • Drug Discovery and Development
  • Neurodegenerative Diseases

Background:

  • Protein aggregation is implicated in numerous human diseases, including Alzheimer's and Huntington's disease.
  • Existing strategies for developing effective protein aggregation inhibitors have faced significant challenges in clinical translation.
  • Protein aggregates exhibit diverse structures and shapes, complicating the development of universal inhibitors.

Purpose of the Study:

  • To develop a novel class of peptide inhibitors targeting early stages of protein aggregation.
  • To investigate the potential of these peptides to inhibit both amorphous and fibrillar protein aggregates.
  • To identify key molecular determinants governing the efficacy of these cross-mechanistic aggregation inhibitors.

Main Methods:

  • Utilized peptide arrays to screen for inhibitors of amorphous aggregation using an aggregation-prone mutant of the Axin tumor suppressor.
  • Optimized peptide sequences based on molecular determinants such as residue composition, hydrophobicity, and distribution.
  • Assessed the inhibitory activity of optimized peptides against Tau fibrillation (Alzheimer's disease) and Huntingtin Exon1 aggregation (Huntington's disease).

Main Results:

  • Identified a family of peptides effective against early-stage amorphous aggregation of Axin.
  • Determined that peptide efficacy relies on specific molecular features (residue composition, hydrophobicity, distribution) rather than sequence.
  • Demonstrated that these peptides inhibit Tau fibrillation and slow Huntingtin Exon1 aggregation, despite sequence and structural differences.

Conclusions:

  • Developed cross-mechanistic, multi-targeting peptide inhibitors effective against diverse protein aggregation pathways.
  • These peptides target dynamic aggregation precursors, offering a novel therapeutic strategy.
  • The identified peptide characteristics provide a foundation for developing drug candidates against a range of protein aggregation diseases.