Helioferin B
* Please be kindly noted products are not for therapeutic use. We do not sell to patients.
| Category | Antibiotics |
| Catalog number | BBF-01332 |
| CAS | 163365-07-9 |
| Molecular Weight | 1135.52 |
| Molecular Formula | C58H106N10O12 |
| Purity | ≥98% |
Online Inquiry
Description
It is produced by the strain of Mycogone rosea DSM 8822. It is a lipopeptide antifungal antibiotic. It has anti-candida albicans, gram-positive bacteria, mycobacterium activity with MIC of 1.5-5.0 μg/mL.
Specification
| Synonyms | Alaninamide, 1-(2-methyl-1-oxooctyl)-L-prolyl-6-hydroxy-4-methyl-8-oxo-2-aminodecanoyl-L-alanyl-2-methylalanyl-L-isoleucyl-L-isoleucyl-2-methylalanyl-N-[2-[(2-hydroxyethyl)methylamino]-1-methylethyl]-2-methyl- |
Properties
| Appearance | White Crystalline Powder |
| Antibiotic Activity Spectrum | Gram-positive bacteria; Fungi; Mycobacteria; Yeast |
| Melting Point | 200-205 °C (dec.) |
Reference Reading
1. The crystal structure of the lipoaminopeptaibol helioferin, an antibiotic peptide from Mycogone rosea
Renate Gessmann, Hans Brückner, Albrecht Berg, Kyriacos Petratos Acta Crystallogr D Struct Biol. 2018 Apr 1;74(Pt 4):315-320. doi: 10.1107/S2059798318001857. Epub 2018 Apr 3.
The crystal structure of the natural nonapeptide antibiotic helioferin has been determined and refined to 0.9 Å resolution. Helioferin consists of helioferin A and B, which contain 2-(2'-aminopropyl)aminoethanol (Apae) and 2-[(2'-aminopropyl)methylamino]ethanol (Amae) at their respective alkanolamine termini. In addition, helioferin contains the unusual amino-acid residues α-aminoisobutyric acid (Aib) and (2S,4S,6S)-2-amino-6-hydroxy-4-methyl-8-oxodecanoic acid (Ahmod). The amino-terminus is capped with 2-methyl-n-1-octanoic acid (M8a). The peptide crystallizes with a 1:1 molar ratio of helioferin A and B in the monoclinic space group C2, with unit-cell parameters a = 34.711, b = 10.886, c = 17.150 Å, β = 93.05°. The peptide backbone folds in a regular right-handed α-helical conformation, with eight intramolecular hydrogen bonds, all but one forming 5→1 interactions. The two aliphatic chains of the fatty-acyl (M8a) and the second residue (Ahmod) extend out of the α-helical structure in opposite directions and lead to a corkscrew-like shape of the peptide molecule. Halogen anions (Cl- and F-) have been co-crystallized with the peptide molecules, implying a positive charge at the aminoalcohol end of the peptide. In the tightly packed crystal the helices are linked head to tail via the anions by electrostatic, hydrogen-bond and van der Waals interactions, forming continuous helical rods. Two nonparallel rods (forming an angle of 118°) interact directly via hydrogen bonds and via the anions, forming a double layer. Successive double layers are held together only via van der Waals contacts. The helical axes of successive double layers are also related by an angle of 118°. The structure of helioferin reported here and the previously determined structure of the homologous leucinostatin A have a total straight length of about 21 Å, indicating a different membrane-modifying bioactivity from that of long-chain, amphiphilic peptaibols.
Recommended Products
| BBF-03755 | Actinomycin D | Inquiry |
| BBF-01693 | Doxorubicin EP Impurity A (Daunorubicin) | Inquiry |
| BBF-03753 | Baicalin | Inquiry |
| BBF-00764 | Cerebroside C | Inquiry |
| BBF-00677 | 3-Amino-3-deoxy-D-glucose | Inquiry |
| BBF-03754 | Castanospermine | Inquiry |
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 ╳
