Abstract

HYDROPHOBIC INTERACTIONS OF YELLOW WASP TOXIN PEPTIDES WITH ION CHANNELS AND ITS EFFECT ON INTEGRITY OF BIOLOGICAL MEMBRANES

Krishna Kumar Prajapati and Ravi Kant Upadhyay*

ABSTRACT

Present review article explains hydrophobic interactions that form during binding of toxin or toxin peptides to ion channels or activated ionic pumps which actively maintain ionic concentration across the plasma membranes. Wasps venom toxins mainly, anoplin a short peptides after binding with a receptor proteins, changes its confirmatory structure. Wasp toxin peptides maintain hydrophobic versus electrostatic interactions with binding to lipid bilayer. These structural changes increase antimicrobial and hemolytic activity, and lipid interactions. Peptides of the mastoparans family showed antimicrobial effects due to presence of net positive charge, amphipathicity and hydrophobicity. Other factors such as peptides length, amino acid substitutions at different positions of the peptide chain, N-terminal acylation and C-terminal deamidation also contribute its interaction with ion channels. Wasp venom toxins such as melittin, phospholipases-A2, hyaluronidases and other bioactive substances directly interacts with cell membranes and disrupt its integrity and generate immune allergic responses. These biological interactions of membrane-peptides complexes are important to analyze both the dynamic properties and pharmacological activities of toxins in solution.

Keywords: Hydrophobic interactions, amphipathicity, transportans-10, Mastoparan-X, G-proteins, Polistes flavus, Anoplius samariensis and Anoplin.