Samarosporin
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| Category | Antibiotics |
| Catalog number | BBF-02861 |
| CAS | 60304-25-8 |
| Molecular Weight | 1458.70 |
| Molecular Formula | C71H107N15O18 |
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Description
It is a peptide antibiotic produced by the strain of Samarospora sp. No. F-7762. It has anti-bacterial, yeast, fungi and protozoa effects, but the effect is not strong. The serum can reduce its activity.
Specification
| IUPAC Name | 3-[(3S,12S,15S,18S,33S,45S)-3,39-dibenzyl-20,46-dihydroxy-39-(hydroxymethyl)-6,6,9,9,24,24,27,27,30,30,42,42-dodecamethyl-33-(2-methylpropyl)-2,5,8,11,14,17,23,26,29,32,35,38,41,44-tetradecaoxo-12-propan-2-yl-1,4,7,10,13,16,22,25,28,31,34,37,40,43-tetradecazatricyclo[43.3.0.018,22]octatetracontan-15-yl]propanamide |
| Canonical SMILES | CC(C)CC1C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N2CC(CC2C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)NC(C(=O)N3CCC(C3C(=O)NC(C(=O)NC(C(=O)NCC(=O)N1)(CC4=CC=CC=C4)CO)(C)C)O)CC5=CC=CC=C5)(C)C)(C)C)C(C)C)CCC(=O)N)O)(C)C)(C)C)(C)C |
| InChI | InChI=1S/C71H107N15O18/c1-38(2)31-44-53(93)78-66(7,8)59(99)82-69(13,14)61(101)83-70(15,16)64(104)86-36-42(88)33-46(86)54(94)75-43(27-28-48(72)90)52(92)77-50(39(3)4)55(95)79-67(9,10)60(100)81-65(5,6)58(98)76-45(32-40-23-19-17-20-24-40)57(97)85-30-29-47(89)51(85)56(96)80-68(11,12)62(102)84-71(37-87,34-41-25-21-18-22-26-41)63(103)73-35-49(91)74-44/h17-26,38-39,42-47,50-51,87-89H,27-37H2,1-16H3,(H2,72,90)(H,73,103)(H,74,91)(H,75,94)(H,76,98)(H,77,92)(H,78,93)(H,79,95)(H,80,96)(H,81,100)(H,82,99)(H,83,101)(H,84,102)/t42?,43-,44-,45-,46-,47?,50-,51-,71?/m0/s1 |
| InChI Key | GWEVIYFFHJZCPV-WHSDTMKSSA-N |
Properties
| Appearance | Colorless Acicular Crystal |
| Antibiotic Activity Spectrum | Fungi; Yeast |
| Melting Point | 255-256.5°C |
| Solubility | Soluble in Methanol |
Reference Reading
1. The crystal structure of samarosporin I at atomic resolution
Renate Gessmann, Danny Axford, Gwyndaf Evans, Hans Brückner, Kyriacos Petratos J Pept Sci. 2012 Nov;18(11):678-84. doi: 10.1002/psc.2454. Epub 2012 Sep 28.
The atomic resolution structures of samarosporin I have been determined at 100 and 293 K. This is the first crystal structure of a natural 15-residue peptaibol. The amino acid sequence in samarosporin I is identical to emerimicin IV and stilbellin I. Samarosporin is a peptide antibiotic produced by the ascomycetous fungus Samarospora rostrup and belongs to peptaibol subfamily 2. The structures at both temperatures are very similar to each other adopting mainly a 3₁₀-helical and a minor fraction of α-helical conformation. The helices are significantly bent and packed in an antiparallel fashion in the centered monoclinic lattice leaving among them an approximately 10-Å channel extending along the crystallographic twofold axis. Only two ordered water molecules per peptide molecule were located in the channel. Comparisons have been carried out with crystal structures of subfamily 2 16-residue peptaibols antiamoebin and cephaibols. The repercussion of the structural analysis of samarosporin on membrane function is discussed.
2. Monitoring the Site-Specific Solid-State NMR Data in Oligopeptides
Jiří Czernek, Jiří Brus Int J Mol Sci. 2020 Apr 13;21(8):2700. doi: 10.3390/ijms21082700.
Reliable values of the solid-state NMR (SSNMR) parameters together with precise structural data specific for a given amino acid site in an oligopeptide are needed for the proper interpretation of measurements aiming at an understanding of oligopeptides' function. The periodic density functional theory (DFT)-based computations of geometries and SSNMR chemical shielding tensors (CSTs) of solids are shown to be accurate enough to support the SSNMR investigations of suitably chosen models of oriented samples of oligopeptides. This finding is based on a thorough comparison between the DFT and experimental data for a set of tripeptides with both 13Cα and 15Namid CSTs available from the single-crystal SSNMR measurements and covering the three most common secondary structural elements of polypeptides. Thus, the ground is laid for a quantitative description of local spectral parameters of crystalline oligopeptides, as demonstrated for the backbone 15Namid nuclei of samarosporin I, which is a pentadecapeptide (composed of five classical and ten nonproteinogenic amino acids) featuring a strong antimicrobial activity.
3. A natural, single-residue substitution yields a less active peptaibiotic: the structure of bergofungin A at atomic resolution
Renate Gessmann, Danny Axford, Hans Brückner, Albrecht Berg, Kyriacos Petratos Acta Crystallogr F Struct Biol Commun. 2017 Feb 1;73(Pt 2):95-100. doi: 10.1107/S2053230X17001236. Epub 2017 Jan 27.
Bergofungin is a peptide antibiotic that is produced by the ascomycetous fungus Emericellopsis donezkii HKI 0059 and belongs to peptaibol subfamily 2. The crystal structure of bergofungin A has been determined and refined to 0.84 Å resolution. This is the second crystal structure of a natural 15-residue peptaibol, after that of samarosporin I. The amino-terminal phenylalanine residue in samarosporin I is exchanged to a valine residue in bergofungin A. According to agar diffusion tests, this results in a nearly inactive antibiotic peptide compared with the moderately active samarosporin I. Crystals were obtained from methanol solutions of purified bergofungin mixed with water. Although there are differences in the intramolecular hydrogen-bonding scheme of samarosporin I, the overall folding is very similar for both peptaibols, namely 310-helical at the termini and α-helical in the middle of the molecules. Bergofungin A and samarosporin I molecules are arranged in a similar way in both lattices. However, the packing of bergofungin A exhibits a second solvent channel along the twofold axis. This latter channel occurs in the vicinity of the N-terminus, where the natural substitution resides.
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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 ╳
