Chrysospermin B

Chrysospermin B

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Category Antibiotics
Catalog number BBF-00331
CAS
Molecular Weight 1912.23
Molecular Formula C91H142N22O23

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Description

It is produced by the strain of Apiocrea chrysosperma Ap101. Chrysospermin B has antibacterial activities against individual gram-positive bacteria (Staphylococcus aureus, Bacillus subtilis), Klebsiella pneumoniae and individual yeasts (Ocher echinoderma, saccharomyces cerevisiae).

Properties

Appearance White Powder
Antibiotic Activity Spectrum Gram-positive bacteria; yeast
Melting Point 250 °C

Reference Reading

1. Effective diameters of ion channels formed by homologs of the antibiotic chrysospermin
V I Ternovsky, P A Grigoriev, G N Berestovsky, R Schlegel, K Dornberger, U Gräfe Membr Cell Biol. 1997;11(4):497-505.
Radii of ion channels formed in the lipid bilayer by 4 homologs of the alamethicin-like antibiotic, chrysospermin, were determined using hydrophilic nonelectrolytes. It is shown that the replacement of isovaline amino acid at position 15 of the polypeptide chain by alpha-aminoisobutyric acid results in the decrease in the channel effective radius from 1.2 +/- 0.15 to 0.94 +/- 0.1 nm and a respective 2.5-fold decrease in channel conductance.
2. Mass spectrometric sequencing of synthetic peptides containing alpha, alpha-dialkylated amino acid residues by MALDI post-source decay analysis
H Wenschuh, D Suckau, U Rapp, M Bienert, F Krause Pept Res. 1996 May-Jun;9(3):122-6.
Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), a method well-suited for mass determination of biomolecules, has been used to analyze fragment ions generated by post-source decay (PSD) of synthetic peptaibols containing high proportions of the sterically hindered amino acids alpha-amino isobutyric acid (Aib) and isovaline (Iva). Since peptaibols do not have a free N-terminal amino group or side chains subject to protonation, the analyzed peptides saturnisporin SA III, trichotoxin A-50 and chrysospermin B were shown to provide preferred N-terminal and C-terminal a, b, and y fragments as sodium adduct. Additionally, a cleavage of the labile Aib-Probond was observed for all peptides investigated. The fragmentation pattern allowed confirmation of the primary structure and, therefore, demonstrated the usefulness of MALDI-PSD mass spectrometry for sequence analysis of the peptaibols.
3. Chrysospermins, new peptaibol antibiotics from Apiocrea chrysosperma Ap101
K Dornberger, W Ihn, M Ritzau, U Gräfe, B Schlegel, W F Fleck, J W Metzger J Antibiot (Tokyo). 1995 Sep;48(9):977-89. doi: 10.7164/antibiotics.48.977.
Four new members of peptaibol antibiotics, designated as chrysospermins A, B, C, and D, were isolated from the mycelium of Apiocrea chrysosperma Ap101 by solvent extraction, silica gel chromatography and preparative recycling HPLC. Their structures as new nonadecapeptides were settled by detailed spectroscopic analysis and chemical degradation experiments. The chrysospermins display antibacterial and antifungal activity, and induce pigment formation by the fungus Phoma destructiva.

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Tip: Chemical formula is case sensitive. C22H30N4O c22h30n40
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