6272-27-1Relevant academic research and scientific papers
Aurones as new porcine pancreatic α-amylase inhibitors
Roshanzamir, Khashayar,Kashani-Amin, Elaheh,Ebrahim-Habibi, Azadeh,Navidpour, Latifeh
, p. 333 - 340 (2019/06/20)
Background: Aurones, (Z)-2-benzylidenebenzofuran-3-one derivatives, are naturally-occurring structural isomers of flavones, with promising pharmacological potential. Methods: In this study, the structural requirements for the inhibition of porcine pancreatic α-amylase by hydroxylated or methoxylated aurone derivatives were investigated by assessing their in vitro biological activities against porcine pancreatic α-amylase. Results: The structure-activity relationship of these inhibitors based on both in vitro and in silico findings showed that the hydrogen bonds between the OH groups of the A or B ring of (Z)-benzylidenebenzofuran-3-one derivatives and the catalytic residues of the binding site are crucial for their inhibitory activities. Conclusion: It seems that the OH groups in aurones inhibit α-amylase in a manner similar to that of OH groups in flavones and flavonols.
Specificity of Calreticulin Transacetylase to acetoxy derivatives of benzofurans: Effect on the activation of platelet Nitric Oxide Synthase
Gupta, Anjali,Priya, Nivedita,Jalal, Sarah,Singh, Prabhjot,Chand, Karam,Raj, Hanumantharao G.,Parmar, Virinder S.,DePass, Anthony L.,Sharma, Sunil K.
experimental part, p. 1180 - 1185 (2011/11/06)
Calreticulin Transacetylase (CRTAase) catalyzes the transfer of acetyl group(s) from polyphenolic acetates (PAs) to functional proteins, such as Glutathione S-transferase (GST), NADPH Cytochrome c reductase and Nitric Oxide Synthase (NOS) resulting in the modulation of biological activities. A comparison of the specificities of the acetoxy derivatives of coumarins, biscoumarins, chromones, flavones, isoflavones and xanthones has been carried out earlier by us with an aim to study the effect of nature and position of the acetoxy groups on the benzenoid ring and the position of the carbonyl group with respect to oxygen/nitrogen heteroatom for the catalytic activity of CRTAase. In this communication for the first time, we have studied the influence of differently substituted benzofurans on the CRTAase activity to study the effect of the replacement of pyran ring of coumarin with furan ring, presence of carbonyl at C-3, substitution of C-3 carbonyl group with acetoxy group and presence of various substituents (OAc/OH/Cl) on the benzenoid ring. It was observed that acetoxy derivatives of benzofurans lead to inhibition of ADP induced platelet aggregation by the activation of platelet Nitric Oxide Synthase catalyzed by CRTAase. Accordingly, the formation of NO in platelets by 3-oxo-2,3-dihydrobenzofuran-6,7-diyl diacetate (3a) was found to be comparable with that of model polyphenolic acetate (PA), 7,8-diacetoxy-4-methylcoumarin (DAMC).
Synthesis and antioxidative activity of 3′,4′,6,7- tetrahydroxyaurone, a metabolite of Bidens frondosa
Venkateswarlu, Somepalli,Panchagnula, Gopala K.,Subbaraju, Gottumukkala V.
, p. 2183 - 2185 (2007/10/03)
3′,4′,6,7-Tetrahydroxyaurone (1a), an aurone isolated from Bidens frondosa, and five analogues (1b-1f) were synthesized from pyrogallol in three steps. The antioxidative activity of 1a-1f was determined by the superoxide free radical and 1,1-diphenyl-2-picrylhydrazyl (DPPH) free radical scavenging methods.
A series of 2(Z)-2-benzylidene-6,7-dihydroxybenzofuran-3[2H]-ones as inhibitors of chorismate synthase
Thomas, Michael G.,Lawson, Chris,Allanson, Nigel M.,Leslie, Bruce W.,Bottomley, Joanna R.,McBride, Andrew,Olusanya, Oyinkan A.
, p. 423 - 426 (2007/10/03)
A series of 2(Z)-2-benzylidene-6,7-dihydroxybenzofuran-3[2H]-ones was identified as potent inhibitors of bacterial chorismate synthase. The 2′-hydroxy-4′-pentoxy analogue 33 is a potent inhibitor of Streptococcus pneumoniae chorismate synthase.
