Abstract:
:A novel 6.6 kDa antifungal peptide (NFAP) from the culture supernatant of the mold, Neosartorya fischeri (anamorf: Aspergillus fischerianus), and its encoding gene were isolated in this study. NFAP is a small, basic and cysteine-rich protein consisting of 57 amino acid residues. It shows 37.9-50% homology to similar proteins described in literature from Aspergillus clavatus, Aspergillus giganteus, Aspergillus niger, and Penicillium chrysogenum. The in silico presumed tertiary structure of NFAP, e.g. the presence of five antiparallel β-sheet connected with filaments, and stabilized by three disulfide bridges, is very similar to those of the defensin-like molecules. NFAP exhibited growth inhibitory action against filamentous fungi in a dose-dependent manner, and maintained high antifungal activity within broad pH and temperature ranges. Furthermore, it exhibited relevant resistance to proteolysis. All these characteristics make NFAP a promising candidate for further in vitro and in vivo investigations aiming at the development of new antifungal compounds.
journal_name
Peptidesjournal_title
Peptidesauthors
Kovács L,Virágh M,Takó M,Papp T,Vágvölgyi C,Galgóczy Ldoi
10.1016/j.peptides.2011.06.022subject
Has Abstractpub_date
2011-08-01 00:00:00pages
1724-31issue
8eissn
0196-9781issn
1873-5169pii
S0196-9781(11)00262-2journal_volume
32pub_type
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