Structural determinants of Neosartorya fischeri antifungal protein (NFAP) for folding, stability and antifungal activity.

ABSTRACT: The recent global challenges to prevent and treat fungal infections strongly demand for the development of new antifungal strategies. The structurally very similar cysteine-rich antifungal proteins from ascomycetes provide a feasible basis for designing new antifungal molecules. The main structural elements responsible for folding, stability and antifungal activity are not fully understood, although this is an essential prerequisite for rational protein design. In this study, we used the Neosartorya fischeri antifungal protein (NFAP) to investigate the role of the disulphide bridges, the hydrophobic core, and the N-terminal amino acids in the formation of a highly stable, folded, and antifungal active protein. NFAP and its mutants carrying cysteine deletion (NFAPΔC), hydrophobic core delet

SUBMITTER: Galgoczy L 

PROVIDER: S-EPMC5434006 | biostudies-literature | 2017 May

REPOSITORIES: biostudies-literature