Bergofungin C
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| Category | Enzyme inhibitors |
| Catalog number | BBF-00135 |
| CAS | |
| Molecular Weight | 1511.80 |
| Molecular Formula | C72H118N16O19 |
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Description
Bergofungin C is a Peptaibols compound produced by Emericellopsis donezkii HKI 0059. It has anti-fungal activity such as Sporibolomy-ces salmonicolor and PenicilltiTn fiotatum. It also moderately inhibits prolyl endopeptidase activity.
Specification
| IUPAC Name | (2S)-2-[[(2S,4R)-1-[2-[[2-[[(2S)-2-[[2-[[(2S)-2-[[2-[[2-[[2-[[(2S)-2-acetamido-3-methylbutanoyl]amino]-2-methylpropanoyl]amino]-2-methylpropanoyl]amino]-2-methylpropanoyl]amino]-3-methylbutanoyl]amino]acetyl]amino]-4-methylpentanoyl]amino]-2-methylpropanoyl]amino]-2-methylpropanoyl]-4-hydroxypyrrolidine-2-carbonyl]amino]-N-[1-[(2S,4R)-4-hydroxy-2-[[1-[[(2S)-1-hydroxy-3-phenylpropan-2-yl]amino]-2-methyl-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]pentanediamide |
| Canonical SMILES | CC(C)CC(C(=O)NC(C)(C)C(=O)NC(C)(C)C(=O)N1CC(CC1C(=O)NC(CCC(=O)N)C(=O)NC(C)(C)C(=O)N2CC(CC2C(=O)NC(C)(C)C(=O)NC(CC3=CC=CC=C3)CO)O)O)NC(=O)CNC(=O)C(C(C)C)NC(=O)C(C)(C)NC(=O)C(C)(C)NC(=O)C(C)(C)NC(=O)C(C(C)C)NC(=O)C |
| InChI | InChI=1S/C72H118N16O19/c1-37(2)29-46(77-50(94)33-74-57(99)51(38(3)4)79-60(102)67(10,11)84-63(105)70(16,17)85-61(103)69(14,15)83-58(100)52(39(5)6)75-40(7)90)54(96)80-68(12,13)62(104)86-72(20,21)65(107)87-34-43(91)31-47(87)55(97)78-45(27-28-49(73)93)53(95)81-71(18,19)64(106)88-35-44(92)32-48(88)56(98)82-66(8,9)59(101)76-42(36-89)30-41-25-23-22-24-26-41/h22-26,37-39,42-48,51-52,89,91-92H,27-36H2,1-21H3,(H2,73,93)(H,74,99)(H,75,90)(H,76,101)(H,77,94)(H,78,97)(H,79,102)(H,80,96)(H,81,95)(H,82,98)(H,83,100)(H,84,105)(H,85,103)(H,86,104)/t42-,43+,44+,45-,46-,47-,48-,51-,52-/m0/s1 |
| InChI Key | AEIHZHIUHVEFKY-VHIGQZLQSA-N |
Properties
| Appearance | White Powder |
| Antibiotic Activity Spectrum | fungi |
| Melting Point | 268-271°C |
Reference Reading
1. An automatic solid-phase synthesis of peptaibols
Claudia U Hjørringgaard, Jan M Pedersen, Thomas Vosegaard, Niels Chr Nielsen, Troels Skrydstrup J Org Chem. 2009 Feb 6;74(3):1329-32. doi: 10.1021/jo802058x.
An automated approach to peptaibols using microwave-assisted solid-phase peptide synthesis is demonstrated with a combination of HBTU and acid fluoride mediated couplings for normal and alpha,alpha-dialkylated amino acids, respectively. The method is utilized for the automated synthesis of several full-length peptaibols, including alamethicin, tylopeptin, ampullosporin, bergofungin, cervinin, trikoningin, trichogin, and peptaibolin, reducing both synthesis time and costs significantly as compared to other approaches. Furthermore, the use of noncommercially available reagents is minimized.
2. Isovaline in naturally occurring peptides: A nondestructive methodology for configurational assignment
Marta De Zotti, Barbara Biondi, Marco Crisma, Claudia U Hjørringgaard, Albrecht Berg, Hans Brückner, Claudio Toniolo Biopolymers. 2012;98(1):36-49. doi: 10.1002/bip.21679. Epub 2011 May 17.
The nonproteinogenic, C(α)-tetrasubstituted, helicogenic, chiral α-amino acid isovaline (Iva) is remarkably spread in the biosphere. Together with its achiral, lower homolog α-aminoisobutyric acid (Aib), it represents a characteristic marker of a class of naturally occurring peptide antibiotics, for which the acronym "peptaibiotics" became established. In these peptides, Iva occurs as the (S)-(= L) or the (R)-(= D) enantiomer, but peptide sequences containing both Iva enantiomers are also common. Here, we applied our recently developed (1)H-NMR method, which enables the nondestructive assignment of the configuration of each Iva residue in a peptide of known helical screw sense, to natural and synthetic peptaibiotics. Our method proved to be generally applicable and provided evidence that, in the peptaibiotic bergofungin A, the Iva(12) configuration is (R) and not (S) as reported previously. Moreover, we extended our NMR method by including a (13)C-NMR parameter. A statistical analysis of the preferred main- and side-chain conformations of the Iva residues in peptides, performed based on their published X-ray diffraction structures, allowed us to provide a sound rationale to the NMR criteria exploited to establish the configuration of this amino acid.
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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 ╳
