Emerimicin IIB
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| Category | Antibiotics |
| Catalog number | BBF-03739 |
| CAS | 79395-85-0 |
| Molecular Weight | 1839.18 |
| Molecular Formula | C90H139N19O22 |
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Description
It is produced by the strain of Emericellopsis microspora. It mainly has activity against gram-positive bacteria and various protozoa. The activity of Emerimicin II is stronger than the Emerimicin III and IV.
Specification
| Synonyms | Zervamicin IIB; N-acetyl-L-tryptophyl-L-isoleucyl-L-glutaminyl-L-isovalyl-L-isoleucyl-L-threonyl-alpha-methyl-alanyl-L-leucyl-alpha-methyl-alanyl-(4R)-4-hydroxy-L-prolyl-L-glutaminyl-alpha-methyl-alanyl-(4R)-4-hydroxy-L-prolyl-alpha-methyl-alanyl-L-prolyl-L-phenylalaninol; Ac-Trp-Ile-Gln-Iva-Ile-Thr-Aib-Leu-Aib-Hyp-Gln-Aib-Hyp-Aib-Pro-Phe-ol; Zervamicin IC, 3-L-glutamine- |
| IUPAC Name | (2S)-2-[[(2S,4R)-1-[2-[[(2S)-2-[[2-[[(2S,3R)-2-[[(2S,3S)-2-[[(2S)-2-[[(2S)-2-[[(2S,3S)-2-[[(2S)-2-acetamido-3-(1H-indol-3-yl)propanoyl]amino]-3-methylpentanoyl]amino]-5-amino-5-oxopentanoyl]amino]-2-methylbutanoyl]amino]-3-methylpentanoyl]amino]-3-hydroxybutanoyl]amino]-2-methylpropanoyl]amino]-4-methylpentanoyl]amino]-2-methylpropanoyl]-4-hydroxypyrrolidine-2-carbonyl]amino]-N-[1-[(2S,4R)-4-hydroxy-2-[[1-[(2S)-2-[[(2S)-1-hydroxy-3-phenylpropan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]carbamoyl]pyrrolidin-1-yl]-2-methyl-1-oxopropan-2-yl]pentanediamide |
| Canonical SMILES | CCC(C)C(C(=O)NC(CCC(=O)N)C(=O)NC(C)(CC)C(=O)NC(C(C)CC)C(=O)NC(C(C)O)C(=O)NC(C)(C)C(=O)NC(CC(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)N3CCCC3C(=O)NC(CC4=CC=CC=C4)CO)O)O)NC(=O)C(CC5=CNC6=CC=CC=C65)NC(=O)C |
| InChI | InChI=1S/C90H139N19O22/c1-19-48(6)68(99-71(117)62(94-51(9)112)40-53-43-93-58-31-26-25-30-57(53)58)78(124)97-60(34-36-67(92)116)73(119)106-90(18,21-3)82(128)101-69(49(7)20-2)79(125)100-70(50(8)111)80(126)105-86(10,11)81(127)98-61(38-47(4)5)74(120)103-89(16,17)84(130)108-44-55(113)41-64(108)76(122)96-59(33-35-66(91)115)72(118)102-88(14,15)85(131)109-45-56(114)42-65(109)77(123)104-87(12,13)83(129)107-37-27-32-63(107)75(121)95-54(46-110)39-52-28-23-22-24-29-52/h22-26,28-31,43,47-50,54-56,59-65,68-70,93,110-111,113-114H,19-21,27,32-42,44-46H2,1-18H3,(H2,91,115)(H2,92,116)(H,94,112)(H,95,121)(H,96,122)(H,97,124)(H,98,127)(H,99,117)(H,100,125)(H,101,128)(H,102,118)(H,103,120)(H,104,123)(H,105,126)(H,106,119)/t48-,49-,50+,54-,55+,56+,59-,60-,61-,62-,63-,64-,65-,68-,69-,70-,90-/m0/s1 |
| InChI Key | ORHLIQNDLPNECR-NPRVXUMGSA-N |
Properties
| Antibiotic Activity Spectrum | Gram-positive bacteria |
| Melting Point | 261°C (dec.) |
| Solubility | Soluble in Methanol |
Reference Reading
1. Modeling the secondary structures of the peptaibols antiamoebin I and zervamicin II modified with D-amino acids and proline analogues
Tarsila G Castro, Nuno M Micaêlo, Manuel Melle-Franco J Mol Model. 2017 Oct 16;23(11):313. doi: 10.1007/s00894-017-3479-5.
Antiamoebin I (AAM-I) and zervamicin II (Zrv-IIB) are peptaibols that exert antibiotic activity through the insertion/disruption of cell membranes. In this study, we investigated how the folding of these peptaibols are affected when some of their native residues are replaced with proline analogues and asymmetrical D-α,α-dialkyl glycines (two classes of noncanonical amino acids). Systematic substitutions of native Aib, Pro, Hyp, and Iva residues were performed to elucidate the folding properties of the modified peptaibols incorporating noncanonical residues. The secondary structure of a peptaibol influences its ability to incorporate into membranes and therefore its function. Our findings reveal that native Zrv-IIB unfolds considerably in water. The presence of Iva and the noncanonical proline analogue cis-3-amino-L-proline (ALP) in both peptaibols induces helical structures. Inserting asymmetric glycines such as α-methyl-D-leucine (MDL) and α-methyl-D-phenylalanine (MDP) into the peptaibols induces folding. This preorganization in water may help to overcome the energy barrier required for peptaibol insertion into the membrane, as well as to facilitate the formation of transmembrane channels. Graphical abstract AAM-I and Zrv-IIB peptidomimetics carrying MDL and ALP noncanonical amino acids, exhibiting improved helical secondary structure in water.
2. Acremotins A-D, peptaibiotics produced by the soil-derived fungus Acremonium persicinum SC0105
Chen Wang, Ping Wu, Lei Yao, Jinghua Xue, Liangxiong Xu, Hanxiang Li, Wangqiu Deng, Xiaoyi Wei J Antibiot (Tokyo). 2018 Nov;71(11):927-938. doi: 10.1038/s41429-018-0086-3. Epub 2018 Aug 8.
Four new peptaibiotics, acremotins A-D (1-4) featuring three α,α-dialkylated amino acid-imino acid motifs and an unreduced C-terminal residue, along with the known peptaibiotic XR586 (5) were isolated from the solid cultures of the soil-derived fungus Acremonium persicinum SC0105. Their primary structures were characterized by detailed analysis of the HRESIMS/MS fragmentation pattern combined with comprehensive interpretation of the 1D and 2D NMR spectroscopic data. The absolute configurations of amino acid residues were determined by the advanced Marfey's method. Sequence alignment result shows that 1-4 are closely related to zervamicin IIB and emerimicin IIA, thus belong to peptaibiotic subfamily-3 (SF3). The three-dimensional (3D) structure of 4 was established by theoretical conformational analysis using the ab initio density functional theory (DFT) method, which, together with the CD spectrum, indicated an amphiphilic and helical structure for 4. 1-5 actively inhibited the growth of gram-positive bacterial pathogens, and amongst them 4 was the most potent compound showing MIC of 12.5 and 6.25 µg/ml against S. aureu and MRSA strains, respectively. 1-5 were also cytotoxic against three human cancer cell lines with IC50 ranging from 1.2 to 21.6 μM.
3. Interaction of zervamicin IIB with lipid bilayers. Molecular dynamics study
Olga V Levtsova, Mikhail Yu Antonov, Tatsina V Naumenkova, Olga S Sokolova Comput Biol Chem. 2011 Feb;35(1):34-9. doi: 10.1016/j.compbiolchem.2010.12.005. Epub 2011 Jan 5.
In this work we have studied the interaction of zervamicin IIB (ZrvIIB) with the model membranes of eukaryotes and prokaryotes using all-atom molecular dynamics. In all our simulations zervamicin molecule interacted only with lipid headgroups but did not penetrate the hydrophobic core of the bilayers. During the interaction with the prokaryotic membrane zervamicin placed by its N-termini towards the lipids and rotated at an angle of 40° relatively to the bilayer surface. In the case of eukaryotic membrane zervamicin stayed in the water and located parallel to the membrane surface. We compared hydrogen bonds between peptide and lipids and concluded that interactions of ZrvIIB with prokaryotic membrane are stronger than those with eukaryotic one. Also it was shown that two zervamicin molecules formed dimer and penetrated deeper in the area of lipid headgroups.
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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 ╳
