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

Amyloid Fibrils03:03

Amyloid Fibrils

11.0K
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,...
11.0K
Amyloid Fibrils03:03

Amyloid Fibrils

6.0K
6.0K
Protein Organization01:13

Protein Organization

151.8K
Overview
151.8K
Protein Organization01:24

Protein Organization

8.2K
Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence....
8.2K
Protein Folding01:25

Protein Folding

9.9K
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...
9.9K
Protein Folding01:22

Protein Folding

124.2K
Overview
124.2K

You might also read

Related Articles

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

Sort by
Same author

Gold- and Silver-Nanoparticle-Embodied Amino Acid-Based Hybrid Sustainable Hydrogel Biomatrices for the Electrocatalytic Reduction of Nitrate to Value-Added Ammonia.

Inorganic chemistry·2026
Same author

The clinical, radiological and genetic spectrum AARS2-related leukoencephalopathy: a case series of 15 patients and review of the literature.

Journal of neurology·2026
Same author

Geometric control of Fe(I) intermediates in CO<sub>2</sub> photoreduction by tetrahedral tripodal phosphine complexes.

Dalton transactions (Cambridge, England : 2003)·2026
Same author

Crystallographic and theoretical insights into a fluorogenic turn-on probe for selective Fe<sup>3+</sup> detection with biomolecular binding and <i>in vitro</i> anticancer studies.

Dalton transactions (Cambridge, England : 2003)·2026
Same author

Chirality Induced Odd-Even Spin Selectivity in Self-Assembled Peptide-Based Helical Nanofibers.

ACS nano·2026
Same author

Metal coordination of thiazole-benzothiazole derivatives improves the antiproliferative efficacy against various human cancer cells: Synthesis, X-ray structures and in silico studies.

European journal of medicinal chemistry·2026

Related Experiment Video

Updated: Nov 8, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.1K

Supramolecular Antiparallel β-Sheet Formation by Tetrapeptides Based on Amyloid Sequence.

Souvik Misra1, Pijush Singh2, Rabindra Nath Mahata1

  • 1Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, P.O.-Botanic Garden, Howrah-711103, West Bengal, India.

The Journal of Physical Chemistry. B
|April 22, 2021
PubMed
Summary

Short peptides composed of aliphatic amino acids self-assemble into antiparallel beta-sheet structures, mimicking amyloidogenic peptides. These findings reveal new insights into peptide self-assembly and amyloid formation.

More Related Videos

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

7.5K
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

981

Related Experiment Videos

Last Updated: Nov 8, 2025

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

13.1K
Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

7.5K
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
08:53

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

981

Area of Science:

  • Biochemistry
  • Structural Biology
  • Materials Science

Background:

  • Self-assembly of short peptides is a key area of research with diverse applications.
  • Truncated peptide fragments from neurodegenerative diseases often adopt beta-sheet structures.
  • Aromatic amino acid-rich fragments show a propensity for beta-sheet formation.

Purpose of the Study:

  • To report the crystal structure of two aliphatic tetrapeptides, Boc-GAII-OMe and Boc-GGVV-OMe.
  • To investigate their self-assembly into beta-sheet structures.
  • To compare their properties with native amyloidogenic peptide fragments.

Main Methods:

  • X-ray crystallography to determine solid-state structures.
  • Analysis of noncovalent interactions, including C-C interactions.
  • Ramachandran plot analysis of torsion angles.
  • Fourier-transform infrared (FT-IR) spectroscopy.
  • Circular dichroism (CD) spectroscopy.
  • Congo Red staining and birefringence analysis.

Main Results:

  • The crystal structures reveal antiparallel beta-sheet self-assembly stabilized by hydrogen bonding and other noncovalent interactions.
  • Peptide 1 exhibits a rare C-C interaction between carbonyl and sp3 carbon atoms.
  • Torsion angles confirm beta-sheet conformation.
  • FT-IR and CD spectroscopy indicate beta-sheet structures in solid-state and aqueous solution, respectively.
  • Congo Red staining shows birefringence, indicating amyloidogenic nature.

Conclusions:

  • Short peptides composed solely of aliphatic amino acids can form beta-sheet structures without aromatic residues.
  • These aliphatic peptides mimic the self-assembly and amyloidogenic properties of native amyloid fragments.
  • The study expands understanding of peptide self-assembly and potential therapeutic targets for neurodegenerative diseases.