ABSTRACT
Modern understanding of natural inhibitors of snake venom toxins has led to a diversied classi-cation of these compounds, and the primary structure of antihemorrhagic proteins allowed them to be assigned to the immunoglobulin supergene, colin/opsonin P35, or to the cystatin families. Phospholipase inhibitors were classied as C-type lectin-like proteins (α-PLIs), molecules bearing leucine-rich repeats (β-PLIs), or presenting a three-ngered conformation (γ-PLIs); a single PLI member of the immunoglobulin supergene family has also been described. This chapter reviews recent developments in understanding the biological, chemical, and physicochemical properties of the isolated inhibitors and their mechanisms of action, as well as the structure-function relationships of these inhibitors. Several classical and state-of-the-art methods for assaying the inhibition of toxin activity and characterizing inhibitors’ composition and interactions are provided. Perspectives on the use of natural inhibitors in the neutralization of venom metalloproteinases and phospholipases A2 are also discussed.
