Related Experiment Video
Updated: May 12, 2026

09:34
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
Peptide self-assembly driven by oxo-ester mediated native chemical ligation
Dnyaneshwar B Rasale1, Indrajit Maity, Maruthi Konda
1Department of Chemistry, Indian Institute of Technology Indore, India.
Summary
Researchers utilized oxo-ester mediated native chemical ligation to create peptide self-assembly, forming supramolecular nanofibers and self-supporting gels for advanced biomaterials.
Area of Science:
- Biochemistry
- Materials Science
- Supramolecular Chemistry
Background:
- Native chemical ligation (NCL) is a powerful tool for peptide synthesis.
- Controlling peptide self-assembly is crucial for developing novel biomaterials.
Purpose of the Study:
- To explore oxo-ester mediated NCL for peptide self-assembly.
- To fabricate supramolecular nanofibers and self-supporting gels.
Main Methods:
- Utilized oxo-ester mediated native chemical ligation (NCL).
- Investigated peptide self-assembly triggered by NCL.
Main Results:
- Successfully generated peptide self-assembly.
- Fabricated supramolecular nanofibers.
- Created self-supporting gels.
Conclusions:
- Oxo-ester mediated NCL is effective for directing peptide self-assembly.
- This method offers a novel route to biomaterials like nanofibers and gels.
Related Concept Videos
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...
Oligosaccharide Assembly
Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...
Multiple sugar molecules that may or may...

