Lugardon K, Chasserot-Golaz S, Kieffer A E, Maget-Dana R, Nullans G, Kieffer B, Aunis D, Metz-Boutigue M H
INSERM Unité 338, IFR37 "Biologie de la Communication Cellulaire," 67084 Strasbourg, France.
Ann N Y Acad Sci. 2002 Oct;971:359-61. doi: 10.1111/j.1749-6632.2002.tb04496.x.
The antifungal peptide named chromofungin is the most active vasostatin-I-derived peptide, corresponding to the sequence 47-66 of chromogranin A. (1)H-NMR analysis revealed that it adopts a helical structure. The mechanism implicated in the interaction of chromofungin with fungi and yeast cells was studied by penetration of monolayers and confocal laser microscopy. Chromofungin is able to interact with the cell wall, to cross the plasma membrane, to accumulate in the microorganism, and to inhibit calcineurin activity.
