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Related Concept Videos

Translocation of Proteins into the Mitochondria01:19

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
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ROS-Responsive Methionine-Containing Amphiphilic Peptides Impart Enzyme-Triggered Phase Transition and Antioxidant

Yoshika Hara1, Ken Yoshizawa1, Atsuya Yaguchi1

  • 1Department of Applied Chemistry, Graduate School of Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Naka-cho, Koganei 184-8588, Tokyo, Japan.

Biomacromolecules
|May 9, 2024
PubMed
Summary
This summary is machine-generated.

Researchers designed self-assembling peptides containing methionine to combat reactive oxygen species (ROS). These peptides form hydrogels that transition to a sol phase when oxidized, offering cellular protection against oxidative stress.

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Oxidative Stress Research

Background:

  • Reactive oxygen species (ROS) are crucial for cell signaling but damaging when overproduced, contributing to aging and mutations.
  • Cellular antioxidant systems utilize redox-active sulfur and transition metals to mitigate ROS.
  • Existing antioxidant strategies require inspiration from natural biological systems.

Purpose of the Study:

  • To design novel methionine-containing self-assembling peptides as a biomaterial responsive to oxidative stress.
  • To investigate the relationship between methionine content and the hydrogel's response to oxidation.
  • To evaluate the protective effects of these peptides against ROS-induced cellular damage.

Main Methods:

  • Synthesis of self-assembling peptides incorporating varying numbers of methionine residues.
  • Characterization of hydrogel formation and gel-to-sol phase transition upon exposure to hydrogen peroxide (H₂O₂).
  • Assessment of peptide sensitivity to H₂O₂ and protection against ROS in cellular models.

Main Results:

  • Methionine-containing peptides successfully formed hydrogels.
  • Hydrogels exhibited a concentration-dependent gel-to-sol phase transition in response to H₂O₂ oxidation.
  • Peptides with higher methionine content demonstrated increased sensitivity to oxidation and enhanced cellular protection.
  • The most effective peptide responded to enzymatically generated H₂O₂.

Conclusions:

  • Developed a novel class of methionine-based supramolecular biomaterials.
  • Demonstrated tunable responsiveness to ROS through peptide design.
  • These biomaterials offer a promising strategy for protecting cells against oxidative stress, including enzymatically generated ROS.