Related Experiment Video
Updated: Oct 26, 2025

07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
13.1K
Order from Disorder with Intrinsically Disordered Peptide Amphiphiles
Guy Jacoby1,2,3, Merav Segal Asher2,3,4, Tamara Ehm1,2,3,5
1Raymond & Beverly Sackler School of Physics & Astronomy, Tel Aviv University, Tel Aviv 6997801, Israel.
Journal of the American Chemical Society
|July 26, 2021
Summary
New intrinsically disordered peptide amphiphiles (IDPA) show a pH-triggered shape change, transforming from spheres to long worms. This transition offers potential for novel drug delivery systems.
Area of Science:
- Biochemistry
- Materials Science
- Nanotechnology
Background:
- Amphiphilic molecules and self-assembled structures are crucial in materials design, biomedicine, and cosmetics.
- Conventional phospholipids and block copolymers face limitations in meeting demands for functional complexity.
- Peptide amphiphiles offer an emerging class of molecules with combined advantages.
Purpose of the Study:
- To introduce novel intrinsically disordered peptide amphiphiles (IDPA).
- To investigate the pH-induced micellar phase transition of these IDPAs.
- To explore the potential of IDPA shape transitions for cargo hold-and-release applications.
Main Methods:
- Synthesis of peptide amphiphiles with intrinsically disordered peptide and dendritic hydrophobic domains.
- Experimental characterization of the pH-induced micellar phase transition.
- Development of a theoretical model to describe the pH-response.
Main Results:
- IDPAs exhibit a sharp pH-induced transition from spherical micelles to elongated worm-like micelles.
- The transition is characterized by low-dispersity spheres at one pH and extremely elongated worms at another.
- A theoretical model was proposed to explain the observed pH-responsive behavior.
Conclusions:
- Intrinsically disordered peptide amphiphiles demonstrate tunable, stimuli-responsive behavior.
- The pH-induced shape transition can be harnessed for cargo hold-and-release applications.
- Tailoring interactions in disordered peptides opens avenues for advanced biomedical applications.
More Related Videos
Related Concept Videos
Intrinsically Disordered Proteins
18.7K
Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
18.7K
Intrinsically Disordered Proteins
2.5K
2.5K
Protein Folding
9.8K
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...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
9.8K
Protein Organization
150.7K
Overview
150.7K
Protein Organization
8.1K
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....
The primary structure of a protein is its amino acid sequence....
8.1K
Amyloid Fibrils
10.9K
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,...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
10.9K

