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Related Concept Videos

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Chirality is the most intriguing yet essential facet of nature, governing life’s biochemical processes and precision. It can be observed from a snail shell pattern in a macroscopic world to an amino acid, the minutest building block of life. Most of the snails around the world have right-coiled shells because of the intrinsic chirality in their genes. All the amino acids present in the human body exist in an enantiomerically pure state, except for glycine - the sole achiral amino acid.
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Related Experiment Video

Updated: Mar 19, 2026

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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A Chirality-Guided Molecular Recognition Strategy for Targeting Intrinsically Disordered Proteins.

Kenta Morita1,2, Shiho Seguchi1, Ayaka Hayashi1

  • 1Department of Chemical Science and Engineering, Graduate School of Engineering, Kobe University, Kobe, Japan.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|March 18, 2026
PubMed
Summary
This summary is machine-generated.

Peptide stereocomplexation, driven by hydrophobic and electrostatic forces, enables targeted inhibition of amyloid beta 42 (Aβ42) aggregation. This strategy offers a novel approach for developing therapeutics against intrinsically disordered proteins.

Keywords:
Alzheimer's diseaseamyloid proteinpeptideself‐assemblystereocomplex

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Drug Discovery

Background:

  • Peptide stereocomplexation is known but sequence-dependent conditions are unclear.
  • Amyloid beta 42 (Aβ42) is a pathological intrinsically disordered protein implicated in neurodegenerative diseases.

Purpose of the Study:

  • To systematically investigate peptide stereocomplexation using short tripeptides.
  • To elucidate sequence-dependent conditions for stereocomplexation.
  • To design a D-peptide targeting Aβ42 based on stereocomplexation insights.

Main Methods:

  • Aggregate formation in mixed aqueous solutions.
  • Single-crystal X-ray diffraction.
  • Calorimetry, simulations, and fluorescence assays.

Main Results:

  • Stereocomplexation was driven by hydrophobic and electrostatic interactions.
  • Racemic crystals were observed via X-ray diffraction.
  • A rationally designed D-peptide inhibited Aβ42 fibrillization and cytotoxicity in cells, outperforming RD2.

Conclusions:

  • Peptide stereocomplexation is a viable strategy for designing sequence-targeting ligands.
  • This approach is effective against intrinsically disordered proteins like Aβ42.
  • Developed D-peptide shows therapeutic potential against Aβ42-related pathologies.