Supporting data for "Molecular dynamics reveals oligomerization and lipid-selective membrane binding of antifungal protein, NFAP2 "

Molecular dynamics input files for the paper. Abstract of the paper: Fungal infections represent an increasing burden in health care worldwide. The Neosartorya (Aspergillus) fischeri antifungal protein 2 (NFAP2) is a small, cysteine-rich, cationic protein with potent anti-Candida activity. Membrane disruption has been demonstrated as its primary mechanism of action, and in previous work we investigated its membrane-binding properties on simple model lipids using a combination of experimental approaches and molecular dynamics simulations. Here, we extend the in-silico studies using physiologically more relevant membrane models of complex compositions including an asymmetric, fungal cell membrane-mimicking bilayer. Results confirm our earlier findings that the 10NCPNNCKHKKG20 region plays a dominant role in membrane binding, however, the C-terminal folded part containing the anchoring Trp42 also contributed significantly in the fungal-mimicking system. To address the pore-formation mechanism assuming protein association, the dimerization/oligomerization propensity of NFAP2 and the membrane-binding behavior of the dimers were examined. NFAP2 was found to form stable dimers in aqueous solution both at high and low ionic strength. In comparison to the monomeric form, the dimers exhibited a broader range of membrane binding modes, although the main lipid contact regions largely overlapped if not involved in protein-protein interactions.