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Protein Complex Assembly

Protein Complex Assembly

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...

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Related Experiment Video

Updated: Sep 15, 2025

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Self-Assembly of Gamma-Modified Peptide Nucleic Acids into Complex Nanostructures in Organic Solvent Mixtures

Published on: June 26, 2020

Nucleobase self-assembly: aggregation, morphological characterization, and toxicity analysis.

Raj Dave¹, Ankita Jaiswal², Ankur Singh³

¹Department of Chemistry, Indrashil University Kadi Mehsana Gujarat India gournidhi@gmail.com nidhi.gour@indrashiluniversity.edu.in.

Nanoscale Advances

|July 16, 2025

Summary

This summary is machine-generated.

This study reveals that aged nucleobases like guanine, cytosine, and thymine self-assemble into toxic, amyloid-like fibrils. These aggregates impair cellular protein clearance, suggesting a new mechanism for inborn errors of metabolism.

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Last Updated: Sep 15, 2025

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Published on: June 26, 2020

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Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Area of Science:

Biochemistry
Molecular Biology
Cell Biology

Background:

Nucleobases are fundamental units of nucleic acids.
Amyloidogenic proteins misfold and aggregate, causing disease.
Inborn errors of metabolism (IEMs) involve metabolic pathway disruptions.

Purpose of the Study:

To investigate the self-assembly and toxicity of guanine, cytosine, and thymine.
To explore the amyloidogenic propensity of unexplored nucleobases.
To understand the role of nucleobase aggregation in IEMs.

Main Methods:

Studied self-assembly of guanine, cytosine, and thymine.
Used Thioflavin T (ThT) dye to detect amyloid-like structures.
Performed MTT assays in RPE-1 cell lines.
Conducted in vivo assays in C. elegans nematodes.

Main Results:

Guanine, cytosine, and thymine form fibrillar assemblies, especially when aged.
Nucleobase aggregates exhibit ThT-binding spectra characteristic of amyloids.
Aggregates are toxic to RPE-1 cells, with aged samples showing higher toxicity.
In vivo assays and heat shock survival assays confirm aggregate toxicity and interference with protein clearance.

Conclusions:

Nucleobases can self-assemble into toxic, amyloid-like structures.
This aggregation mechanism contributes to toxicity in inborn errors of metabolism.
Further research into nucleobase amyloidogenesis is warranted for understanding IEMs.