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Editorial [Hot Topic: Structural-Functional Studies of Animal Toxins (Guest Editor: Marcos R.M. Fontes)]

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Animal venoms are a rich and complex mixture of toxic and pharmacologically active proteins and peptides. Due to this broad range of biological functions, these biomolecules have been the subject of hundreds of scientific articles in different research fields, including biochemistry, biophysics, pharmacology, toxicology and medicine. This issue is focused on the structural and functional aspects of some animal toxins which could be important for understanding their biological mechanisms and pharmacological properties.

In many rural areas in Asia, Latin American and Africa the envenomation by snakes, scorpions, spiders and other venomous animals causes thousands of deaths. This is a serious problem of public health as a result of the associated chronic morbidity (e.g., amputation, deformation and renal failure) causing significant social and economic impact [1]. Even though the patients are treated with anti-venom agents, many of them present serious and permanent physical damage. The deeper study of these compounds could be very important for the development of new and more efficient treatments against animal venoms.

Additionally, the pharmacological properties of the peptides and proteins from animal venoms lead to them being used as effective drugs for hypertension, thrombosis and other diseases and are potential drugs for a great variety of diseases including cancer, Alzheimer's, Parkinson's and inflammatory disorders.

This issue of Protein and Peptide Letters contains eleven manuscripts describing structural and functional analysis of different proteins and peptides from snakes, spiders, scorpions and wasps. The first review by Magro and colleagues discusses the importance of the oligomeric conformation of snake venoms phospholipases A2 in their biological function. The second review by Lomonte and co-workers is focused in the Phospholipases A2 homologues from snake venoms, emphasizing their biological activities in vivo and in vitro. The review by Oliveira et al. is centered in Calcium-independent membrane damage by snake venom Phospholipases A2 homologues. In the next article, dos Santos et al. analyzed the controversial subject of the biological assembly for Phospholipases A2 homologues from snake venoms focused in the myotoxicity and catalytic inactivity. Rodrigues et al. studied the snake venom Phospholipases A2 as an antitumoral agent while de Paula et al. reviewed snake venoms from the pharmacological and structural perspective. The functional and structural characteristics of snake venom Lamino acid oxidades are reviewed by Zuliani et al. The review by Soares and Oliveira is focused in the structure-function relationship of the glycoproteins from snake venoms. Cologna et al. presents a general revision of the pharmacological and physiological proprieties of the venom from the most important scorpion specie in South America. The review of dos Santos and Dias et al. describe a proteomic analysis of different proteins from Loxosceles intermedia spider venom. In the last article, Monteiro et al. review wasp venom components and their biological effects. Finally, I hope this issue could have new and useful information about different biological molecules from animal venoms.

Document Type: Research Article


Publication date: August 1, 2009

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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