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Related Concept Videos

Molecular Chaperones and Protein Folding03:00

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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Nuclear protein sorting is the selective trafficking of histones, polymerases, gene regulatory proteins into the nucleus and exporting RNAs and ribosomes to the cytosol. It is a tightly controlled process that regulates gene expression within a cell.
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Proteins that regulate transcription can do so either via direct contact with RNA Polymerase or through indirect interactions facilitated by adaptors, mediators, histone-modifying proteins, and nucleosome remodelers. Direct interactions to activate transcription is seen in bacteria as well as in some eukaryotic genes. In these cases, upstream activation sequences are adjacent to the promoters, and the activator proteins interact directly with the transcriptional machinery. For example, in...
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Updated: Jan 13, 2026

In Vitro Characterization of Histone Chaperones using Analytical, Pull-Down and Chaperoning Assays
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G4 Oligonucleotide-Based Chaperones of Heterogeneous Nuclear Ribonucleoprotein A1.

Elizaveta Malakhova1, Julia Svetlova1, Iuliia Pavlova1

  • 1Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine of Federal Medical Biological Agency, Malaya Pirogovskaya, 1a, 119435 Moscow, Russia.

International Journal of Molecular Sciences
|October 29, 2025
PubMed
Summary

Researchers designed novel oligonucleotide chaperones for hnRNP A1, a protein implicated in neurodegenerative diseases. These chaperones effectively prevent the formation of toxic protein aggregates, offering a promising therapeutic strategy for brain disorders.

Keywords:
G-quadruplexaggregationchaperoneproteinopathyribonucleoprotein

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Area of Science:

  • Biochemistry
  • Neuroscience
  • Drug Discovery

Background:

  • Heterogeneous nuclear ribonucleoproteins (hnRNPs) form aggregates in neurodegenerative diseases.
  • Pharmacological chaperones are being explored for neuroprotection by preventing protein aggregation.

Purpose of the Study:

  • To rationally design and characterize novel oligonucleotide chaperones targeting hnRNP A1.
  • To investigate the efficacy of these chaperones in preventing hnRNP A1 aggregation and condensate formation.

Main Methods:

  • Rational design combining RRM and G-quadruplex motifs for hnRNP A1 binding.
  • Oligonucleotide backbone modifications to enhance binding and stability.
  • Microscale thermophoresis for affinity assessment.
  • Fluorimetry and microscopy for evaluating chaperone activity and inhibition of aggregation.

Main Results:

  • Modified oligonucleotide chaperones demonstrated improved affinity and activity towards hnRNP A1.
  • The leading chaperone bound hnRNP A1 at micromolar concentrations.
  • Over 90% inhibition of hnRNP A1 condensate and amyloid-like fibril assembly was achieved.

Conclusions:

  • Rational design of oligonucleotide chaperones is a viable strategy for targeting hnRNP A1.
  • These novel chaperones show significant potential for preventing the pathological aggregation of hnRNP A1.
  • Oligonucleotide chaperones represent a promising therapeutic avenue for neurodegenerative diseases.