Cobra Cytotoxins: Structure, Evolution, Biological Activities, Underlying Molecular Mechanism, and Derived Bioactive Analogues
A special issue of Toxins (ISSN 2072-6651). This special issue belongs to the section "Animal Venoms".
Deadline for manuscript submissions: 31 May 2024 | Viewed by 11658
Special Issue Editor
Interests: cobra venom; proteomics; cytolytic peptides; antiproliferative activity; structure-functional relationship; antimicrobial peptide; template-based design of bioactive peptides; lipid/peptide interactions; apoptosis; action synergism
Special Issue Information
Dear Colleagues,
Cobra cytotoxins (cardiotoxins) are representatives of the three-finger proteins, which constitute a substantial part of cobra and coral snake venom. They have a long history of investigation, with nearly half a century having elapsed since they were first isolated and the amino acid composition of the first representatives was determined. The views on the evolution and spatial structure of these molecules, their biological activity, and underlying mechanisms are scattered over this long period. This Special Issue is devoted to concentrating all these data and examining them with modern eyes, removing possible controversies. Moreover, newly emerging topics, including pharmacological applications of these molecules and derived analogues, are welcome.
Dr. Peter V. Dubovskii
Guest Editor
Manuscript Submission Information
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Keywords
- three-finger toxins
- cobra cytotoxins
- biological activity
- mechanism of activity
Planned Papers
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
Title: Diversity of cobra cytotoxins: Revelation from venomics on structural and functional complexity
Authors: Choo Hock Tan; Kae Yi Tan
Affiliation: Faculty of Medicine, University of Malaya, Malaysia.
Abstract: Abstract (TENTATIVE): Cytotoxins of the three-finger toxin family are virtually found in the venom of every cobra (Naja) species. These toxins, although sharing a common protein motif, have structural variability that impacts their biological activities. Furthermore, the type and relative abundance of cytotoxins in each cobra venom can vary between and even within species. Recent venomic studies unravel the diversity of cobra cytotoxins, elucidating the complexity of their compositions, structures and biological functions. Notably, the substitution of certain amino acid residues drastically changes in the toxicity spectrum, distinguishing the molecules into different subtypes, such as the P type with strong membrane-damaging properties, the S type with relatively lower toxicity, and the emergent H type with negligible cytotoxicity but potentially channel-targeting activity – the nomenclature of “cytotoxin” is, therefore, perhaps debatable. The distribution of different cytotoxin forms within venom largely conforms to the cobras’ phylogeny, indicating evolutionary significance in the context of predation and defence for species survival. In cobra envenoming, antivenoms generally have weak neutralization effects against cytotoxin-induced tissue necrosis; hence, small-molecule inhibitors should be explored as the next promising adjunct treatment. The cobra cytotoxins, with their structural and functional versatility, are also promising sources for future bioprospecting and drug discovery research.
