Chrysospermin C
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| Category | Antibiotics |
| Catalog number | BBF-00332 |
| CAS | |
| Molecular Weight | 1912.23 |
| Molecular Formula | C91H142N22O23 |
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Description
It is produced by the strain of Apiocrea chrysosperma Ap101. Chrysospermin C 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. The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles
R Anders, O Ohlenschläger, V Soskic, H Wenschuh, B Heise, L R Brown Eur J Biochem. 2000 Mar;267(6):1784-94. doi: 10.1046/j.1432-1327.2000.01177.x.
Chrysospermin C is a 19-residue peptaibol capable of forming transmembrane ion channels in phospholipid bilayers. The conformation of chrysospermin C bound to dodecylphosphocholine micelles has been solved using heteronuclear NMR spectroscopy. Selective 15N-labeling and 13C-labeling of specific alpha-aminoisobutyric acid residues was used to obtain complete stereospecific assignments for all eight alpha-aminoisobutyric acid residues. Structures were calculated using 339 distance constraints and 40 angle constraints obtained from NMR data. The NMR structures superimpose with mean global rmsd values to the mean structure of 0. 27 A (backbone heavy atoms) and 0.42 A (all heavy atoms). Chrysospermin C bound to decylphosphocholine micelles displays two well-defined helices at the N-terminus (residues Phe1-Aib9) and C-terminus (Aib13-Trp-ol19). A slight bend preceding Pro14, i.e. encompassing residues 10-12, results in an angle of approximately 38 degrees between the mean axes of the two helical regions. The bend structure observed for chrysospermin C is compatible with the sequences of all 18 long peptaibols and may represent a common 'active' conformation. The structure of chrysospermin C shows clear hydrophobic and hydrophilic surfaces which would be appropriate for the formation of oligomeric ion channels.
2. Differences in membrane pore formation by peptaibols
Pavel A Grigoriev, Brigitte Schlegel, Matthias Kronen, Albrecht Berg, Albert Härtl, Udo Gräfe J Pept Sci. 2003 Nov-Dec;9(11-12):763-8. doi: 10.1002/psc.502.
The efficiencies of membrane pore formation by 14 naturally occurring peptaibols and two structurally modified ampullosporins were compared using an artificial bilayer membrane model. Major differences were found in the dependence on peptide sequences and the constituting amino acids. Alamethicin F-30, chrysospermins C/D, paracelsin and texenomycin A displayed higher activity by several orders of magnitude in comparison with smaller peptaibols containing < 17 amino acids such as ampullosporins, trichofumins. bergofungins and cephaibols. Biological activities such as the induction of pigment formation by the fungus Phoma destructiva and long acting hypothermia and depression of locomotor activity in mice were correlated with moderate membrane permeabilization. No or weak membrane activities corresponded with biological inactivity. Highly membrane-active structures such as alamethicin F-30, chrysospermin C, texenomycin A and paracelsin A displayed antibiotic effects against the fungus and toxicity in mice.
3. A solution NMR study of the selectively 13C, 15N-labeled peptaibol chrysospermin C in methanol
R Anders, H Wenschuh, V Soskic, S Fischer-Frühholz, O Ohlenschläger, K Dornberger, L R Brown J Pept Res. 1998 Jul;52(1):34-44. doi: 10.1111/j.1399-3011.1998.tb00650.x.
The conformation of the 19-residue peptaibol chrysospermin C in methanol has been investigated by NMR spectroscopy using selective 15N and 13C labeling of the alpha-aminoisobutyric acid (Aib) residues. Complete 1H and 13C sequential assignments, including stereospecific assignments for the heavily overlapped resonances from the two Cbeta methyl groups of the eight Aib residues, are reported for a peptaibol for the first time. An Aib residue followed by a Pro is an exception to previous suggestions regarding stereospecific assignment of the two Cbeta methyl groups of Aib residues. Local nuclear Overhauser effects and 3J(HNC') and 3J(HNCbeta) scalar couplings indicate that the phi angles of the Aib residues are restricted sterically to local conformations consistent with right-handed helices. Despite these constraints on the eight Aib residues, the NMR data for chrysospermin C in methanol are generally most consistent with an ensemble of transient conformations, including backbone conformations inconsistent with helical structures. Initial NMR measurements for chrysospermin C bound to micelles suggest structural and dynamic differences relative to alamethicin bound to micelles which may be related to differences in gating voltages for formation of ion channels.
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Bio Calculators
* Our calculator is based on the following equation:
Concentration (start) x Volume (start) = Concentration (final) x Volume (final)
It is commonly abbreviated as: C1V1 = C2V2
* Total Molecular Weight:
g/mol
Tip: Chemical formula is case sensitive. C22H30N4O √ c22h30n40 ╳
