Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum.

@article{Batta2009FunctionalAO,
  title={Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum.},
  author={Gyula Batta and Ter{\'e}z Barna and Zolt{\'a}n G{\'a}sp{\'a}ri and Szabolcs S{\'a}ndor and Katalin E. K{\"o}v{\'e}r and Ulrike Binder and Bettina Sarg and Lydia Kaiserer and Anil Kumar Chhillar and Andrea Eigentler and {\'E}va Leiter and Nikoletta Heged{\"u}s and Istv{\'a}n P{\'o}csi and Herbert Lindner and Florentine Marx},
  journal={The FEBS journal},
  year={2009},
  volume={276 10},
  pages={2875-90}
}
Penicillium antifungal protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, antifungal protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to… CONTINUE READING