Related Experiment Video
Updated: Dec 9, 2025

05:24
Author Spotlight: Improving the Production of Self-Assembling Fibers and Peptide Hydrogels for Superior Biocompatibility
Published on: September 6, 2024
1.6K
Disassembling peptide-based fibres by switching the hydrophobic-hydrophilic balance
Joris T Meijer1, Marloes J A G Henckens1, Inge J Minten1
1Toernooiveld 1, 6525 ED, Nijmegen, The Netherlands. D.Lowik@science.ru.nl.
Soft Matter
|September 9, 2020
Abstract:
Amyloid-like model peptides, modified on the N-terminus with an alkyl tail and on the C-terminus with a PEG chain, yielded fibres that were susceptible to triggered disassembly by removal of the alkyl chain, which affected the hydrophobic-hydrophilic balance.
More Related Videos
Related Concept Videos
Peptide Bonds
81.0K
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...
81.0K
Protein Folding
10.5K
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...
10.5K

