@article { ISI:000359173900007,
	title = {Biochemical, structural and functional diversity between two digestive alpha-amylases from helicoverpa armigera},
	journal = {Biochimica Et Biophysica Acta-General Subjects},
	volume = {1850},
	number = {9},
	year = {2015},
	month = {SEP},
	pages = {1719-1728},
	publisher = {ELSEVIER SCIENCE BV},
	address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS},
	abstract = {<p>Background: Helicoverpa armigera (Lepidoptera) feeds on various plants using diverse digestive enzymes as one of the survival tool-kit. The aim of the present study was to understand biochemical properties of recombinant alpha-amylases of H. armigera viz., HaAmy1 and HaAmy2. Methods: The open reading frames of HaAmy1 and HaAmy2 were cloned in Pichia pastoris and expressed heterologously. Purified recombinant enzymes were characterized for their biochemical and biophysical attributes using established methods. Results: Sequence alignment and homology modeling showed that HaAmy1 and HaAmy2 were conserved in their amino acid sequences and structures. HaAmy1 and HaAmy2 showed optimum activity at 60 degrees C; however, they differed in their optimum pH. Furthermore, HaAmy2 showed higher affinity for starch and amylopectin whereas HaAmy1 had higher catalytic efficiency. HaAmy1 and HaAmy2 were inhibited to the same magnitude by a synthetic amylase inhibitor (acarbose) while wheat amylase inhibitor showed about 2-fold higher inhibition of HaAmy1 than HaAmy2 at pH 7 while 6-fold difference at pH 11. Interactions of HaAmy1 and HaAmy2 with wheat amylase inhibitor revealed 2:1 stoichiometric ratio and much more complex interaction with HaAmy1. Conclusions: The diversity of amylases in perspective of their biochemical and biophysical properties, and their differential interactions with amylase inhibitors signify the potential role of these enzymes in adaptation of H. armigera on diverse plant diets. General significance: Characterization of digestive enzymes of H. armigera provides the molecular basis for the polyphagous nature and thus could assist in designing future strategies for the insect control. (C) 2015 Elsevier B.V. All rights reserved.</p>},
	keywords = {alpha-amylases, Amylase inhibitors, Digestive enzymes, Enzyme activity, Helicoverpa armigera},
	issn = {0304-4165},
	doi = {10.1016/j.bbagen.2015.04.008},
	author = {Bhide, Amey J. and Channale, Sonal M. and Patil, Sucheta S. and Gupta, Vidya S. and Ramasamy, Sureshkumar and Giri, Ashok P.}
}
@article {47164,
	title = {Baicalein suppresses repeat tau fibrillization by sequestering oligomers},
	journal = {Archives of Biochemistry and Biophysics},
	volume = {675},
	year = {2019},
	month = {OCT},
	pages = {108119},
	type = {Article},
	abstract = {<p>Alzheimer{\textquoteright}s disease (AD) is a neurodegenerative disorder caused by protein misfolding, aggregation and accumulation in the brain. A large number of molecules are being screened against these pathogenic proteins but the focus for therapeutics is shifting towards the natural compounds as aggregation inhibitors, mainly due to their minimum adverse effects. Baicalein is a natural compound belonging to the class of flavonoids isolated from the Chinese herb Scutellaria baicalensis. Here we applied fluorescence, absorbance, microscopy, MALDI-TOF spectrophotometry and other biochemical techniques to investigate the interaction between Tau and Baicalein in vitro. We found the aggregation inhibitory properties of Baicalein for the repeat Tau. Overall, the potential of Baicalein in dissolving the preformed Tau oligomers as well as mature fibrils can be of utmost importance in therapeutics for Alzheimer{\textquoteright}s disease.</p>
},
	keywords = {Alzheimer disease, Baicalein, Microtubule assembly, Paired helical filaments, Protein aggregation, tau protein},
	issn = {0003-9861},
	doi = {10.1016/j.abb.2019.108119},
	author = {Sonawane, Shweta Kishor and Balmik, Abhishek Ankur and Boral, Debjyoti and Ramasamy, Sureshkumar and Chinnathambi, Subashchandrabose}
}
