Pore-forming proteins and peptides are ubiquitous in living organisms. They play a central role in bacterial pathogenesis, immune response, venomous attack and innate immunity, by which means they are used to attack and eliminate other organisms. They have the extraordinary property of having two stable structural states. One corresponds to the secreted, soluble, diffusible, and usually monomeric form. The other, adopted only upon cellular attack, is a membrane inserted, channel shaped, and usually oligomeric form. Since membrane insertion is self-assisted and does not require a chaperon or dedicated protein machinery, these molecules represent a gold mine for biochemists and biophysicists interested in the molecular steps leading to membrane insertion and channel formation. As self-assembling entities, capable of punching holes of well-defined size in a lipid membrane, they have found a wealth of applications ranging from cell controlled permeabilisation to intracellular drug delivery, and from the creation of chimeric antitumoral immunotoxins to the preparation of sophisticated elements for biosensors of metal ions or genetic material. Pore-forming Peptides and Protein Toxins provides an essential source of information for graduate students and academic and industrial researchers in the fields of biochemistry, biophysics, toxicology and the pharmaceutical sciences.