Proteomic Analysis and Functional Characterization of Venom

Dear Colleagues,

Studies conducted over the past 50 years have revealed the diversity of animal venoms’ chemical composition, and further research is increasingly exploring the synergic and/or individual effects of toxins. Improvements in modern instrumentation have supported large-scale measurement of animal venom proteomes, such as:

• Purification of proteins and peptides by liquid chromatography (LC);
• Analysis of selective proteins by enzyme-linked immunosorbent assay (ELISA) and Western blotting;
• Separation of complex protein samples by sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE), two-dimensional gel electrophoresis (2-DE) and two-dimensional differential gel electrophoresis (2D-DIGE) techniques;
• Mass spectrometry (MS) for analyzing the complex protein mixtures with higher sensitivity;
• Free and stable isotopes labeling (ICAT, SILAC and iTRAQ) techniques for quantitative proteomic;
• X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy providing three-dimensional (3D) structure of protein, furthering the understanding of its biological function;
• Bioinformatics tools for 3D structure prediction, protein domain and motif analysis, rapid analysis of protein–protein interaction, evolutionary relationship and data analysis of MS.

This Special Issue will cover recent progress in proteomics techniques for the proteome and functional characterization of animal venoms and/or individual toxins to promote an improved understanding of the mechanisms of envenomation and/or to reveal bioactive molecules for the development of novel drugs.

Dr. Lucilene Delazari dos Santos
Dr. Juliana Pavan Zuliani
Prof. Dr. Andreimar M. Soares
Guest Editors

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