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The protein α-hemolysin (α-HL) is a self-assembling exotoxin that binds to the membrane of a susceptible host cell. In this paper, experimental studies show that cyrtominetin (CTM) can inhibit the hemolytic activity of α-HL. To understand how CTM can affect hemolytic activity, molecular dynamics simulations were carried out for α-HL-CTM complex and these results were compared with the crystal structure of monomeric α-HL. With this approach, the analysis revealed that the inhibition of CTM involves CTM directly binding to α-HL. Due to the binding of CTM, the conformation of the critical "Loop" region was restrained. This mechanism was confirmed by the experimental data. These findings indicate that CTM hinders the lysis activity of α-HL through a novel mechanism., (Copyright © 2013 Elsevier Masson SAS. All rights reserved.)

In this study, hemolysis, Western blot, and real-time RT-PCR assays were performed to evaluate silibinin's activity against S. aureus α-toxin secretion. In addition, live/dead cell staining and lactate dehydrogenase activity assays were introduced to examine the influence of silibinin on α-toxin-induced cell injury in human alveolar epithelial cells. Furthermore, we tested the influence of silibinin on S. aureus pneumonia in a mouse model. We show that silibinin inhibits the expression of α-toxin in a dose-dependent manner and alleviates α-toxin-induced lung cell injury. The IC50 of silibinin that inhibits the hemolytic activity of S. aureus was 14.33 µg/mL for strain 8325-4. Moreover, this compound provides effective protection on the lung injury of staphylococcal pneumonia., (Georg Thieme Verlag KG Stuttgart · New York.)