Browsing by Author "Salar, Uzma"

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    Chalcones and Bis-Chalcones Analogs as DPPH and ABTS Radical Scavengers
    (Bentham Science Publishers, 2021) Bale, Adebayo Tajudeen; Salar, Uzma; Khan, Khalid Mohammed; Chigurupati, Sridevi; Fasina, Tolulope; Ali, Farman; Ali, Muhammad; Nanda, Sekhar Sitanshu; Taha Muhammad; Perveen, Shahnaz
    A number of synthetic scaffolds, along with natural products, have been identified as potent antioxidants. The present study deals with the evaluation of varyingly substituted, medicinally distinct class of compounds “chalcones and bis-chalcones” for their antioxidant potential.
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    Chalcones and bis-chalcones: As potential α-amylase inhibitors; synthesis, in vitro screening, and molecular modelling studies
    (Academic Press Inc., 2018-05-07) Bale, Adebayo Tajudeen; Khan, Khalid Mohammed; Salar, Uzma; Chigurupati, Sridevi; Fasina, Tolulope; Ali, Farman; Kanwal; Abdul Wadood; Taha, Muhammad; Nanda, Sekhar Sitanshu; Ghufran Mehreen; Perveen, Shahnaz
    Despite of a diverse range of biological activities associated with chalcones and bis-chalcones, they are still neglected by the medicinal chemist for their possible α-amylase inhibitory activity. So, the current study is based on the evaluation of this class for the identification of new leads as α-amylase inhibitors. For that purpose, a library of substituted chalcones 1–13 and bis-chalcones 14–18 were synthesized and characterized by spectroscopic techniques EI-MS and 1H NMR. CHN analysis was carried out and found in agreement with the calculated values. All compounds were evaluated for in vitro α-amylase inhibitory activity and demonstrated good activities in the range of IC50 = 1.25 ± 1.05–2.40 ± 0.09 µM as compared to the standard acarbose (IC50 = 1.04 ± 0.3 µM). Limited structure–activity relationship (SAR) was established by considering the effect of different groups attached to aryl rings on varying inhibitory activity. SMe group in chalcones and OMe group in bis-chalcones were found more influential on the activity than other groups. However, in order to predict the involvement of different groups in the binding interactions with the active site of α-amylase enzyme, in silico studies were also conducted.