Metabolites-BOC Sciences

Acarbose - CAS 56180-94-0

Catalog number: BBF-00538

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Catalog Number BBF-00538
CAS 56180-94-0
Description Acarbose is an inhibitor of alpha-glucosidase isolated from Actinoplance sp., used to treat type 2 diabetes.
Related CAS1221158-13-9 (sulfate)
Molecular Formula C25H43NO18
Molecular Weight 645.61
Synonyms Amylostatin J; Bay g 5421; α-GHI; Glucobay; 4,6-dideoxy-4-{[(1S,4S,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino}-alpha-D-glucopyranosyl-(1→4)-alpha-D-glucopyranosyl-(1→4)-beta-D-glucopyranose
IUPAC Name (3R,4R,5S,6R)-5-[(2R,3R,4R,5S,6R)-5-[(2R,3R,4S,5S,6R)-3,4-dihydroxy-6-methyl-5-[[(1S,4R,5S,6S)-4,5,6-trihydroxy-3-(hydroxymethyl)cyclohex-2-en-1-yl]amino]oxan-2-yl]oxy-3,4-dihydroxy-6-(hydroxymethyl)oxan-2-yl]oxy-6-(hydroxymethyl)oxane-2,3,4-triol
Canonical SMILES CC1C(C(C(C(O1)OC2C(OC(C(C2O)O)OC3C(OC(C(C3O)O)O)CO)CO)O)O)NC4C=C(C(C(C4O)O)O)CO
InChI InChI=1S/C25H43NO18/c1-6-11(26-8-2-7(3-27)12(30)15(33)13(8)31)14(32)19(37)24(40-6)43-22-10(5-29)42-25(20(38)17(22)35)44-21-9(4-28)41-23(39)18(36)16(21)34/h2,6,8-39H,3-5H2,1H3/t6-,8+,9-,10-,11-,12-,13+,14+,15+,16-,17-,18-,19-,20-,21-,22-,23?,24-,25-/m1/s1
InChI Key XUFXOAAUWZOOIT-UGEKTDRHSA-N
Boiling Point 971.6°C at 760 mmHg
Melting Point 165-170°C
Purity >95% by HPLC
Density 1.74 g/cm3
Solubility Soluble in Water, Methanol, Ethanol, DMF, DMSO
Appearance White Powder
Storage Store at -20°C
1.Characterization of two coleopteran α-amylases and molecular insights into their differential inhibition by synthetic α-amylase inhibitor, acarbose.
Channale SM1, Bhide AJ1, Yadav Y1, Kashyap G1, Pawar PK2, Maheshwari VL3, Ramasamy S4, Giri AP5. Insect Biochem Mol Biol. 2016 Apr 27;74:1-11. doi: 10.1016/j.ibmb.2016.04.009. [Epub ahead of print]
Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran α-amylases viz. Callosobruchus chinensis α-amylase (CcAmy) and Tribolium castaneum α-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous α-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran α-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor-binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin.
2.Reply to 'Long-term use of acarbose and CV event: confusing finding from mega data bank'.
Chang CH1,2,3, Chang YC3,4,5, Lin JW3,6, Chuang LM1,2,3. Diabet Med. 2016 May 2. doi: 10.1111/dme.13145. [Epub ahead of print]
We appreciate the comments on the discrepancy among the studies raised by Wu et al. However, the study designs and comparators for the acarbose treatment group in the three studies are obviously different. The first study by Chen et al. compared the risk of developing cardiovascular disease (CVD) among patients with Type 2 diabetes receiving various durations and doses of acarbose and those never receiving acarbose [1]. This study did not distinguish between acarbose monotherapy and combination therapy or between first-line acarbose therapy and second-line acarbose therapy. This article is protected by copyright. All rights reserved.
3.Important Aspects of Post-Prandial Antidiabetic Drug, Acarbose.
Singla RK, Singh R, Dubey AK1. Curr Top Med Chem. 2016 Apr 14. [Epub ahead of print]
Acarbose, a well known and efficacious α-amylase and α-glucosidase inhibitor, is a post-prandial acting antidiabetic drug. DNS-based α-amylase inhibitory assays showed that use of acarbose at concentrations above 125 µg/ml resulted in release of reducing sugar in the reaction, an unexpected observation. Objective of the present study was to design experimental strategies to address this unusual finding. Acarbose was found to be susceptible to thermo-lysis. Further, besides being an inhibitor, it could also be hydrolyzed by porcine pancreatic α-amylase, but had weaker affinity for α-amylase compared to starch. GRIP docking was done for the mechanistic analysis of the active site in the enzyme for substrate, inhibitor and, inhibitor's metabolite (K2). Interaction between acarbose and α-amylase involved significant hydrogen binding compared to that of starch, producing a stronger enzyme-inhibitor complex. Further, docking analysis led us to predict the site on α-amylase where the inhibitor (acarbose) bound more tightly, which possibly affected the binding and hydrolysis of starch exerting its effective anti-diabetic function.
4.Comparison of acarbose and metformin therapy in newly diagnosed type 2 diabetic patients with overweight and/or obese.
Sun W1, Zeng C2, Liao L1, Chen J1, Wang Y3. Curr Med Res Opin. 2016 Apr 7:1-34. [Epub ahead of print]
OBJECTIVE: To compare the efficacy of acarbose and metformin in overweight and/or obese patients with newly diagnosed type 2 diabetes mellitus (T2DM).
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