Allosamidin
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| Category | Enzyme inhibitors |
| Catalog number | BBF-00662 |
| CAS | 103782-08-7 |
| Molecular Weight | 622.62 |
| Molecular Formula | C25H42N4O14 |
| Purity | 99% |
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Description
It is produced by the strain of Streptomyces sp. Chitinase specific inhibitor.
Specification
| Synonyms | A82516; A-82516; beta-D-Allopyranoside, 2-(dimethylamino)-3a,5,6,6a-tetrahydro-4-hydroxy-6-(hydroxymethyl)-4H-cyclopentoxazol-5-yl 2-(acetylamino)-4-O-(2-(acetylamino)-2-deoxy-beta-D-allopyranosyl)-2-deoxy-, (3aalpha,4beta,5beta,6alpha,6aalpha)-; Allosamidine; A 82516; 1,2-Dideoxy-2'-dimethylamino-alpha-D-glucopyranoso-[2,1-d]-DELTA2'-thiazoline; CHEMBL118668; DTXSID90883122; BDBM50331851; ZINC53683592; DB04628; LS-171885; C05346; W-200706; Q27095365; (3aR,4R,5R,6S,6aS)-2-(dimethylamino)-4-hydroxy-6-(hydroxymethyl)-4,5,6,6a-tetrahydro-3aH-cyclopenta[d][1,3]oxazol-5-yl 2-(acetylamino)-4-O-[2-(acetylamino)-2-deoxy-beta-D-allopyranosyl]-2-deoxy-beta-D-allopyranoside |
| IUPAC Name | N-[(2S,3R,4S,5S,6R)-2-[(2R,3S,4S,5R,6R)-6-[[(3aR,4R,5R,6S,6aS)-2-(dimethylamino)-4-hydroxy-6-(hydroxymethyl)-4,5,6,6a-tetrahydro-3aH-cyclopenta[d][1,3]oxazol-5-yl]oxy]-5-acetamido-4-hydroxy-2-(hydroxymethyl)oxan-3-yl]oxy-4,5-dihydroxy-6-(hydroxymethyl)oxan-3-yl]acetamide |
| Canonical SMILES | CC(=O)NC1C(C(C(OC1OC2C(OC(C(C2O)NC(=O)C)OC3C(C4C(C3O)N=C(O4)N(C)C)CO)CO)CO)O)O |
| InChI | InChI=1S/C25H42N4O14/c1-8(33)26-14-17(36)16(35)11(6-31)39-23(14)42-22-12(7-32)40-24(15(19(22)38)27-9(2)34)41-21-10(5-30)20-13(18(21)37)28-25(43-20)29(3)4/h10-24,30-32,35-38H,5-7H2,1-4H3,(H,26,33)(H,27,34)/t10-,11+,12+,13+,14+,15+,16+,17-,18+,19-,20-,21+,22+,23-,24-/m0/s1 |
| InChI Key | MDWNFWDBQGOKNZ-XYUDZHFQSA-N |
Properties
| Density | 1.780±0.10 g/cm3 (Predicted) |
Reference Reading
1. Preparation of allosamidin and demethylallosamidin photoaffinity probes and analysis of allosamidin-binding proteins in asthmatic mice
Yosuke Sato, Shigeo Suzuki, Seiko Muraoka, Naoya Kikuchi, Naotaka Noda, Takafumi Matsumoto, Hiromasa Inoue, Hiromichi Nagasawa, Shohei Sakuda Bioorg Med Chem. 2011 May 15;19(10):3054-9. doi: 10.1016/j.bmc.2011.04.012. Epub 2011 Apr 13.
Allosamidins, metabolites of Streptomyces with strong inhibitory activities toward family 18 chitinases, show a variety of biological activities in various organisms. We prepared photoaffinity and biotinylated probes of allosamidin and demethylallosamidin, the N-demethyl derivative that shows much stronger anti-asthmatic activity than allosamidin. Mild acid hydrolysis of allosamidins afforded mono-amine derivatives, which were amidated to prepare probes with a photoactivatable aryl azide and/or biotin moieties. The derivatives with an N-acyl group at C-2 of the D-allosamine residue at the non-reducing end of allosamidins inhibited Trichoderma chitinase as strongly as the original compounds. Since the target of allosamidins in asthma is unclear, photoaffinity probes were used to analyze allosamidin-binding proteins in bronchoalveolar lavage (BAL) fluid in IL-13-induced asthmatic mice. Ym1, a chitinase-like protein, was identified as the main allosamidin-binding protein among proteins whose expression was upregulated by IL-13 in BAL fluid. Binding of allosamidins with Ym1 was confirmed by the experiments with photoaffinity probes and recombinant Ym1.
2. Recent progress on synthesis and activities of allosamidin and its analogues
Gangliang Huang Mini Rev Med Chem. 2012 Jun;12(7):665-70. doi: 10.2174/138955712800626700.
The pseudotrisaccharide allosamidin 1 is a potent family-18 chitinase inhibitor, and it demonstrates biological activities against insects and fungi. Recent development for the synthesis and activities of compound 1 and its analogues was reviewed. Huang et al. described the solid-phase synthesis of allosamidin 1 and its analogues, which were obtained by iterative glycosylation reactions, catalytic hydrogenation, acetylation, and deacetylation, respectively. It indicated that di-N-acetyl-β-chitobiosyl allosamizoline was strongly against insect chitinase from Bombyx mori. Withers and his coworkers have synthesized chitobiose and chitotriose thiazolines, which exhibit chitinase inhibition activity.
3. The roles of three Serratia marcescens chitinases in chitin conversion are reflected in different thermodynamic signatures of allosamidin binding
Jamil Baban, Salima Fjeld, Shohei Sakuda, Vincent G H Eijsink, Morten Sørlie J Phys Chem B. 2010 May 13;114(18):6144-9. doi: 10.1021/jp909801x.
Binding of allosamidin to the three family 18 chitinases of Serratia marcescens has been studied using isothermal titration calorimetry (ITC). Interestingly, the thermodynamic signatures of allosamidin binding were different for all three chitinases. At pH 6.0, chitinase A (ChiA) binds allosamidin with a K(d) value of 0.17 +/- 0.06 microM where the main part of the driving force is due to enthalpic change (DeltaH(r) degrees = -6.2 +/- 0.2 kcal/mol) and less to entropic change (-TDeltaS(r) degrees = -3.2 kcal/mol). A large part of DeltaH is due to allosamidin stacking with Trp(167) in the -3 subsite. Binding of allosamidin to both chitinase B (ChiB) (K(d) = 0.16 +/- 0.04 microM) and chitinase C (ChiC) (K(d) = 2.0 +/- 0.2 microM) is driven by entropy (DeltaH(r) degrees = 3.8 +/- 0.2 kcal/mol and -TDeltaS(r) degrees = -13.2 kcal/mol for ChiB and DeltaH(r) degrees = -0.6 +/- 0.1 and -TDeltaS(r) degrees = -7.3 kcal/mol for ChiC). For ChiC, the entropic term is dominated by changes in solvation entropy (DeltaS(conf) = 1 cal/K.mol and DeltaS(solv) = 31 cal/K.mol), while, for ChiB, changes in conformational entropy dominate (DeltaS(conf) = 37 cal/K x mol and DeltaS(solv) = 15 cal/K x mol). Corresponding values for ChiA are DeltaS(conf) = 4 cal/K x mol and DeltaS(solv) = 15 cal/K x mol. These remarkable differences in binding parameters reflect the different architectures of the catalytic centers in these enzymes that are adapted to different types of actions: ChiA and ChiB are processive enzymes that move in opposite directions, meaning that allosamidin binds in to "product" subsites in ChiB, while it binds to polymer-binding subsites in ChiA. The values for ChiC are compatible with this enzyme being a nonprocessive endochitinase with a much more open and solvated substrate-binding-site cleft.
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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 ╳
