Bioactive Molecules in the Control of Oxidative Stress and Oxidative Stress-Related Diseases

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Molecular Medicine".

Deadline for manuscript submissions: 15 December 2024 | Viewed by 1585

Special Issue Editor

Department of Advanced Biomedical Research, University of Yamanashi, Chuo Shi, Japan
Interests: antioxidants; bioactive molecules; ROS; redox signaling; oxidative stress-related diseases

Special Issue Information

Dear Colleagues,

Oxidative stress is implicated in the pathogenesis of many diseases. This Special Issue will explore the potential of bioactive molecules obtained from natural, dietary, and endogenous sources to modulate oxidative stress and its associated pathologies. This Special Issue aims to compile cutting-edge research elucidating the antioxidant, anti-inflammatory, and cytoprotective mechanisms of these biomolecules. Contributions will cover recent findings related to the capabilities of these molecules to regulate free radical generation, influence redox signaling pathways and antioxidant defenses, and mitigate oxidative damage in cells, tissues and organs. Authors are invited to submit original research articles and authoritative reviews detailing the actions, molecular targets, and therapeutic potential of specific bioactive molecules against oxidative stress and oxidative stress-related diseases. By disseminating these discoveries, this Special Issue seeks to highlight bioactive molecules with promise regarding the prevention or deceleration of the progression of pathologies linked to oxidative stress.

Dr. Jian Yao
Guest Editor

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Keywords

  • antioxidants
  • bioactive molecules
  • ROS
  • redox signaling
  • oxidative stress-related diseases

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Published Papers (1 paper)

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Research

12 pages, 1694 KiB  
Article
Apigenin Provides Structural Protection to Human Fibrinogen against Nitrosative Stress: Biochemical and Molecular Insights
by Aisha Farhana, Abdullah Alsrhani, Yusuf Saleem Khan, Mohammad Salahuddin, Mohammed Ubaidullah Sayeed and Zafar Rasheed
Biomolecules 2024, 14(5), 576; https://doi.org/10.3390/biom14050576 - 13 May 2024
Cited by 1 | Viewed by 1002
Abstract
Background: Peroxynitrite (ONOO) is an oxidant linked with several human pathologies. Apigenin, a natural flavonoid known for its health benefits, remains unexplored in relation to ONOO effects. This study investigated the potential of apigenin to structurally protect fibrinogen, an essential [...] Read more.
Background: Peroxynitrite (ONOO) is an oxidant linked with several human pathologies. Apigenin, a natural flavonoid known for its health benefits, remains unexplored in relation to ONOO effects. This study investigated the potential of apigenin to structurally protect fibrinogen, an essential blood clotting factor, from ONOO-induced damage. Methods: Multi-approach analyses were carried out where fibrinogen was exposed to ONOO generation while testing the efficacy of apigenin. The role of apigenin against ONOO-induced modifications in fibrinogen was investigated using UV spectroscopy, tryptophan or tyrosine fluorescence, protein hydrophobicity, carbonylation, and electrophoretic analyses. Results: The findings demonstrate that apigenin significantly inhibits ONOO-induced oxidative damage in fibrinogen. ONOO caused reduced UV absorption, which was reversed by apigenin treatment. Moreover, ONOO diminished tryptophan and tyrosine fluorescence, which was effectively restored by apigenin treatment. Apigenin also reduced the hydrophobicity of ONOO-damaged fibrinogen. Moreover, apigenin exhibited protective effects against ONOO-induced protein carbonylation. SDS-PAGE analyses revealed that ONOOtreatment eliminated bands corresponding to fibrinogen polypeptide chains Aα and γ, while apigenin preserved these changes. Conclusions: This study highlights, for the first time, the role of apigenin in structural protection of human fibrinogen against peroxynitrite-induced nitrosative damage. Our data indicate that apigenin offers structural protection to all three polypeptide chains (Aα, Bβ, and γ) of human fibrinogen. Specifically, apigenin prevents the dislocation or breakdown of the amino acids tryptophan, tyrosine, lysine, arginine, proline, and threonine and also prevents the exposure of hydrophobic sites in fibrinogen induced by ONOO. Full article
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