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Related Experiment Video

Updated: Nov 17, 2025

Directed Assembly of Elastin-like Proteins into defined Supramolecular Structures and Cargo Encapsulation In Vitro

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Published on: April 8, 2020

Peptide Assemblies Mimicking Chaperones for Protein Trafficking.

Dongsik Yang¹, Hongjian He¹, Beom Jin Kim¹

¹Department of Chemistry, Brandeis University, 415 South Street, Waltham, Massachusetts 02454, United States.

Bioconjugate Chemistry

|February 17, 2021

Summary

This summary is machine-generated.

Negatively charged peptides self-assemble into micelles, demonstrating a novel method for trafficking histone proteins to cellular mitochondria. This supramolecular approach offers insights into mimicking chaperone functions and controlling protein interactions.

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Last Updated: Nov 17, 2025

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In Situ Monitoring of Transiently Formed Molecular Chaperone Assemblies in Bacteria, Yeast, and Human Cells

Published on: September 2, 2019

Area of Science:

Biochemistry
Supramolecular Chemistry
Cell Biology

Background:

Self-assembly of peptides is well-studied, but negatively charged peptides (NCPs) remain underexplored.
Acidic sequences are common in intrinsically disordered regions of histone chaperones.

Purpose of the Study:

To investigate the self-assembly of NCPs for histone protein trafficking.
To explore a supramolecular strategy for controlling cellular processes.

Main Methods:

Peptide synthesis with glutamic acid (E)-repeats.
pH-dependent self-assembly studies in solution.
Circular dichroism spectroscopy to analyze peptide conformation.
Cellular assays to assess histone 2B (H2B) trafficking to mitochondria.

Main Results:

Glutamic acid-repeat peptides self-assemble into micelles at neutral or basic pH.
Increasing pH promotes disordered and alpha-helical conformations.
NCP assemblies are non-toxic and successfully traffic H2B to mitochondria.
Self-assembly, stereochemistry, and acidic repeats are crucial for H2B trafficking.

Conclusions:

This study presents the first example of peptide assemblies for protein trafficking.
NCP assemblies offer a supramolecular approach for cellular process control.
Findings provide insights for mimicking chaperones and modulating protein-protein interactions.