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Updated: Apr 19, 2026

Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly

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Published on: February 6, 2020

Programming pH-triggered self-assembly transitions via isomerization of peptide sequence.

Arijit Ghosh¹, Eric T Dobson, Christian J Buettner

¹Department of Chemistry and Biochemistry, The Ohio State University , Columbus, Ohio 43210, United States.

Langmuir : the ACS Journal of Surfaces and Colloids

|December 5, 2014

Summary

Altering amino acid sequence in peptides changes their self-assembly. Moving a hydrophobic amino acid can control pH-triggered formation of nanofibers versus spherical micelles.

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Area of Science:

Biochemistry
Materials Science
Supramolecular Chemistry

Background:

Amino acid order dictates protein folding and material structure.
Stimuli-responsive peptide self-assembly is crucial for advanced materials.
Sequence isomerization for controlled self-assembly is underexplored.

Purpose of the Study:

To investigate the impact of hydrophobic amino acid position on pH-triggered peptide self-assembly.
To explore sequence isomerization as a strategy for controlling peptide nanostructures.

Main Methods:

Synthesized amphiphilic peptides with varying isoleucine positions.
Utilized pH-triggered self-assembly experiments.
Characterized resulting nanostructures (nanofibers, spherical micelles).

Main Results:

Moving isoleucine from the palmitoyl tail shifted pH-triggered assembly.
Nanofiber formation was favored over spherical micelles with altered isoleucine position.
Transition pH shifted to more basic conditions by 2 units.

Conclusions:

Peptide sequence isomerization offers a novel method to program self-assembly.
Hydrophobic amino acid placement significantly influences pH-responsive nanostructure formation.
Findings enable precise control over peptide-based material architectures.