Related Experiment Video
Updated: Jan 20, 2026
09:22
Self-assembling Morphologies Obtained from Helical Polycarbodiimide Copolymers and Their Triazole Derivatives
Published on: February 7, 2017
8.2K
Directional assembly of a stapled α-helical peptide
Kuan Hu1, Feng Yin, Ziyuan Zhou
1State Key Laboratory of Chemical Oncogenomics, School of Chemical Biology and Biotechnology, Shenzhen Graduate School, Peking University, Shenzhen 518055, China. lizg@pkusz.edu.cn.
Chemical Communications (Cambridge, England)
|August 16, 2019
Summary
Scientists developed a new oxidation method to create stapled peptides that self-assemble into nanostructures. These peptide nanostructures can deliver small interfering RNA (siRNA) into cancer cells and release it in reductive environments.
Area of Science:
- Biomaterials Science
- Supramolecular Chemistry
- Nanotechnology
Background:
- De novo design of peptide-based self-assemblies is a growing field but presents significant challenges.
- Controlling peptide structure and assembly is crucial for developing functional nanomaterials.
Purpose of the Study:
- To develop an oxidation-triggered method for peptide stapling and subsequent self-assembly.
- To create novel peptide nanostructures capable of targeted cargo delivery.
Main Methods:
- Designed a self-assembling peptide sequence (Fmoc-R(RCEX)2-NH2) with flanking cysteine residues.
- Induced α-helical structure formation via oxidation-triggered disulfide bond formation (i/i+4 stapling).
- Characterized self-assembly into nanorod and nanovesicle structures.
Main Results:
- Oxidation successfully stapled the peptide, inducing a conformational change from random coil to α-helix.
- The stapled peptide self-assembled into ordered nanorod and nanovesicle structures.
- The assembled peptide nanostructures demonstrated effective delivery of small interfering RNA (siRNA) into cancer cells.
Conclusions:
- Oxidation-triggered peptide stapling is a viable strategy for de novo design of self-assembling nanomaterials.
- The resulting peptide nanostructures can be utilized for siRNA delivery, with cargo release triggered by reductive environments.
- This approach offers a promising platform for developing advanced drug/gene delivery systems.
Related Concept Videos
02:43Peptide Bonds
82.4K
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...
82.4K
02:15Protein and Protein Structure
87.0K
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme...
A protein's shape is critical to its function. For example, an enzyme...
87.0K
02:41Protein Complex Assembly
16.7K
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...
16.7K
01:10α-Alkylation of Ketones via Enolate Ions
3.8K
Ketones with α protons are deprotonated by strong bases like lithium diisopropylamide (LDA) to form enolate ions. The anion is stabilized by resonance, and its hybrid structure exhibits negative charges on the carbonyl oxygen and the α carbon. This ambident nucleophile can attack an electrophile via two possible sites: the carbonyl oxygen, known as O-attack, or the α carbon, known as C-attack. The nucleophilic attack via the carbanionic site is preferred. This is due to the...
3.8K
01:09Directing Effect of Substituents: meta-Directing Groups
5.8K
Substituents on the benzene ring that direct an incoming electrophile to undergo substitution at the meta position are called meta directors. All meta directors either have a positive charge on the atom directly bonded to the ring or a partial positive charge. These groups function by withdrawing electrons from the ring through inductive and resonance effects. Consider the carbocation intermediates formed upon the addition of an electrophile on nitrobenzene at the...
5.8K
02:50Spindle Assembly
4.2K
Spindle assembly occurs through three, often coexisting, pathways – the centrosome-mediated pathway, the chromatin-mediated pathway, and the microtubule-mediated pathway – collectively contributing to form a robust spindle apparatus.
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
In most cells, centrosomes are the primary microtubule nucleation centers. In the centrosome-mediated pathway, the G2-prophase transition triggers centrosome maturation and increased microtubule nucleation. Progressive nucleation results in a...
4.2K