Gastric cancer is a pathological condition induced by the bacteria Helicobacter pylori. Targeting the key virulence factors of H. pylori causing gastric cancer is a promising method for treating gastric cancer. Recently, research has been focused on analyzing the adrenergic, cholinergic, and anti-cancer properties of their venom proteins. Testing the anti-cancer activity of the lethal proteins in the venom of P. volitans provides a bioactive compound for cancer treatment. Still, it is also helpful to eliminate the ecological imbalance caused by these fish in the marine environment. This study focuses on an in silico approach using Z-dock to analyze the bioactive prospective of the venom proteins of P. volitans against the essential virulence proteins of H. pylori responsible for inducing cancer. Our in silico docking study using a computational model of the venom proteins and H. pylori proteins has displayed the possible interactions between these proteins. The results revealed that P. volitans hyaluronidase and PV toxin's venom proteins effectively interact with H. pylori proteins Cag A, Cag L, GGT, Cag D, and urease that may be promising proteins in cancer therapy.
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1007/s12010-021-03763-x | DOI Listing |
Curr Opin Chem Biol
January 2025
Department of Biological Sciences, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal Bypass Road, Bhauri, Bhopal, 462066, Madhya Pradesh, India; Department of Chemistry, Indian Institute of Science Education and Research (IISER) Bhopal, Bhopal Bypass Road, Bhauri, Bhopal, 462066, Madhya Pradesh, India. Electronic address:
Animal venom contains ion channel-targeting peptide toxins that inflict paralysis or pain. The high specificity and potency of these toxins for their target ion channels provides enticing opportunities for their deployment as tools in channel biology. Mechanistic studies on toxin-mediated ion channel modulation have yielded landmark breakthroughs in our understanding of channel architectures and gating mechanisms.
View Article and Find Full Text PDFChem Biodivers
January 2025
Federal Fluminense University: Universidade Federal Fluminense, Molecular and Cellular Biology, . Prof. Marcos Waldemar de Freitas Reis - São Domingos, Bloco M, Campus Gragoatá, 24210-201, Niteroi, BRAZIL.
Snakebite envenomation is a public health issue that can lead to mortality and physical consequences. It is estimated that 5.4 million venomous snake bites occur annually, with 130,000 deaths and 400,000 amputations.
View Article and Find Full Text PDFTrans R Soc Trop Med Hyg
January 2025
Metabolomics and Proteomics Laboratory, Department of Biological Science and Engineering, Maulana Azad National Institute of Technology, Bhopal 462003, India.
Snake venom proteins have long been recognized for their therapeutic potential. Proteogenomic strategies, integrating transcriptomics and proteomics, have emerged as powerful tools for identifying and characterizing venom proteins for the development of novel therapeutic agents. Analytical techniques like mass spectrometry and next-generation sequencing enable comprehensive analysis, identifying key venom components and their variants.
View Article and Find Full Text PDFTrans R Soc Trop Med Hyg
January 2025
Pharm-Biotechnology and Traditional Medicine Centre (PHARMBIOTRAC), Faculty of Medicine, Mbarara University of Science and Technology, Mbarara 40006, Uganda.
Snake venom, a complex mixture of proteins, has attracted human attention for centuries due to its associated mortality, morbidity and other therapeutic properties. In sub-Saharan Africa (SSA), where snakebites pose a significant health risk, understanding the genetic variability of snake venoms is crucial for developing effective antivenoms. The wide geographic distribution of venomous snake species in SSA countries demonstrates the need to develop specific and broad antivenoms.
View Article and Find Full Text PDFTrans R Soc Trop Med Hyg
January 2025
Conse jo Nacional de Investigaciones Científicas y Técnicas (CONICET), Instituto de Química Básica y Aplicada del Nordeste Argentino (IQUIBA-NEA), CP3400 Corrientes, Argentina.
Background: The WHO states that antivenom is the only safe and effective treatment to neutralize snake venom. Snakebite antivenom typically involves horse hyperimmunization with crude venom and Freund's adjuvant.
Methods: In the current work, we analyzed the ascorbyl palmitate liquid crystal structure with snake protein or PLA2, the carrier charge capacity, and we evaluated the immune response induced by the enzyme P9a(Cdt-PLA2) formulated in a nanostructure using CpG-ODN, determining the titer of IgG antibodies.
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!