Related Experiment Video
Updated: Jul 2, 2026

07:26
Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
Published on: November 21, 2013
Bioactive molecular sheets from self-assembly of polymerizable peptides
Kyung-Soo Moon1, Eunji Lee, Yong-beom Lim
1Center for Supramolecular Nano-Assembly, Department of Chemistry, Yonsei University, Shinchon 134, Seoul 120-749, Korea.
Summary
Polymerizable peptides form 2D sheets for efficient, non-toxic cellular cargo delivery. These novel molecular objects offer a safer alternative to existing nanostructures.
Area of Science:
- Biomaterials science
- Nanotechnology
- Cellular biology
Background:
- Self-assembling peptides offer potential for novel nanomaterial fabrication.
- Existing nanostructures can exhibit toxicity and limited cargo delivery efficiency.
Purpose of the Study:
- To develop and characterize novel 2D molecular objects from polymerizable peptides.
- To evaluate the efficacy and safety of these 2D structures for cellular cargo delivery.
Main Methods:
- Self-assembly of polymerizable peptides in bulk solution.
- Covalent fixation to create stable 2D molecular objects.
- In vitro assessment of cargo delivery into living cells.
- Cytotoxicity evaluation compared to non-polymerized nanostructures.
Main Results:
- Demonstrated self-assembly of polymerizable peptides into unique sheet-like 2D structures.
- Successfully produced covalently fixed 2D molecular objects.
- Achieved efficient cargo delivery into living cells.
- Exhibited nearly non-toxic profiles compared to non-polymerized counterparts.
Conclusions:
- Polymerizable peptides can be engineered into stable, 2D molecular objects with significant potential in nanomedicine.
- These 2D structures represent a promising platform for safe and effective intracellular cargo delivery.
Related Concept Videos
Protein Complex Assembly
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types. Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Peptide Bonds
A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Assembly of Cytoskeletal Filaments
Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
Protein Organization
Overview
Protein Organization
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.
Protein Folding
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...

