Pyrularia Thionin

Abstract

There is an increasing interest in the interaction of small basic peptides with cellular and synthetic membranes, both in terms of the initial binding process and subsequent alterations seen in the phospholipid bilayer order and organization. In terms of its general structure and mode of action with cellular membranes, pyrularia thionin (PT) can be directly compared to both melittin and cardiotoxin (CTX), two other toxic peptides which have been extensively studied. It is generally accepted that all three peptides show electrostatic binding to membranes through strongly charged regions of the peptide, followed by insertion of a hydrophobic portion of the molecule into the membrane bilayer, causing alterations of phospholipid order and structure. The properties of melittin (1,2) and CTX (3,4) have been reviewed.KeywordsPowdery MildewPhosphatidic AcidP388 CellSnake VenomPhospholipid BilayerThese keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.