Pyrularia Thionin

Physical Properties, Binding to Phospholid Bilayers and Cellular Responses
  • Leo P. Vernon
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 391)

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.

Keywords

Permeability Toxicity Tyrosine Hydrocarbon Polypeptide 

Abbreviations

CTX

cardiotoxin

PA

phosphatic acid

PC

phosphatidylcholine

PS

Phosphatidylserine

PLA2

Phospholipase A2

PT

pyrularia thionin

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Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • Leo P. Vernon
    • 1
  1. 1.Chemistry DepartmentBrigham Young UniversityProvoUSA

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