Structural and biological characterization of chromofungin, the antifungal chromogranin A (47-66)-derived peptide.
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.
Lugardon
K
K
INSERM Unité 338, IFR37 "Biologie de la Communication Cellulaire," 67084 Strasbourg, France.
Chasserot-Golaz
S
S
Kieffer
A E
AE
Maget-Dana
R
R
Nullans
G
G
Kieffer
B
B
Aunis
D
D
Metz-Boutigue
M H
MH
D000528:Alternaria / Q000378:metabolism; D000935:Antifungal Agents / Q000737:chemistry; D001232:Aspergillus fumigatus / Q000378:metabolism; D065095:Calcineurin Inhibitors; D002135:Calcium-Binding Proteins / Q000378:metabolism; D037282:Calreticulin; D002176:Candida albicans / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism; D053379:Chromogranin A; D002864:Chromogranins / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D010455:Peptides / Q000737:chemistry* / Q000494:pharmacology; D017434:Protein Structure, Tertiary; D012261:Ribonucleoproteins / Q000378:metabolism
D000935:Antifungal Agents; C506150:CHGA protein, human; D065095:Calcineurin Inhibitors; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D053379:Chromogranin A; D002864:Chromogranins; D010446:Peptide Fragments; D010455:Peptides; D012261:Ribonucleoproteins; C437333:chromofungin; C121986:vasostatin