@article { ISI:000229558600004,
	title = {Characterization of two midgut proteinases of helicoverpa armigera and their interaction with proteinase inhibitors},
	journal = {Journal of Insect Physiology},
	volume = {51},
	number = {5},
	year = {2005},
	month = {MAY},
	pages = {513-522},
	publisher = {PERGAMON-ELSEVIER SCIENCE LTD},
	type = {Article},
	address = {THE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLAND},
	abstract = {<p>Two serine proteinases from the midgut of Helicoverpa armigera have been partially purified and characterized. One proteinase, HGP-1, was capable of hydrolyzing a synthetic substrate of elastase and was inhibited by elastatinal. The second proteinase, HGP-2, was inhibited by a trypsin inhibitor. Molecular weights of HGP-1 and HGP-2 were approximately 26.0 and 29.0 kDa, respectively. Both the proteinases exhibited alkaline pH optima in the range of 10-11. Furthermore, interaction of HGP-1 and HGP-2 with proteinase inhibitors (PIs) from host and non-host plants was studied. HGP-1 was not only insensitive to a PI from chickpea (host) but was also able to degrade it. The same PI from chickpea was able to inhibit over 50\% activity of HGP-2. On the contrary, PIs from potato (non-host) showed strong inhibition of both, HGP-1 and HGP-2 and also demonstrated protection of chickpea seed proteins from digestion by both the HGPs. These results could provide important clues in designing strategies for sustainable use of plant PIs in developing insect-tolerant transgenic plants. (C) 2005 Elsevier Ltd. All rights reserved.</p>},
	keywords = {elastase, Helicoverpa armigera gut proteinases, insect-resistant plants, plant proteinase inhibitors},
	issn = {0022-1910},
	doi = {10.1016/j.jinsphys.2004.12.004},
	author = {Telang, M. A. and Giri, Ashok P. and Sainani, Mohini N. and Gupta, Vidya S.}
}
@article {47118,
	title = {Molecular elucidation of pancreatic elastase inhibition by baicalein},
	journal = {Journal of Biomolecular Structure \& Dynamics},
	volume = {40},
	year = {2022},
	month = {JUL},
	pages = {5759-5768},
	type = {Article},
	abstract = {<p>
	The serine protease, elastase exists in various forms and plays diverse roles in the human body. Pharmacological inhibition of elastase has been investigated for its therapeutic role in managing conditions such as diabetes, pneumonia and arthritis. Sivelestat, a synthetic molecule, is the only elastase inhibitor to have been approved by any major drug regulatory authority (PMDA, in this case) - but still has failed to attain widespread clinical usage owing to its high price, cumbersome administration and obscure long-term safety profile. In order to find a relatively better-suited alternative, screening was conducted using plant flavonoids, which yielded baicalein, a molecule that showed robust inhibition against Pancreatic Elastase inhibition (IC50: 3.53 mu M). Other than having a considerably lower IC(50)than sivelestat, baicalein is also cheaper, safer and easier to administer. While MicroScale Thermophoresis validated baicalein-elastase interaction, enzyme-kinetic studies, molecular docking and molecular dynamic simulation revealed the mode of inhibition to be non-competitive. Baicalein exhibited binding to a distinct allosteric site on the enzyme. The current study demonstrates the elastase inhibition properties of baicalein in an in-vitro and in-silico environment.</p>
},
	keywords = {Baicalein, elastase, Enzyme inhibition, molecular interaction, sivelestat},
	issn = {0739-1102},
	doi = {10.1080/07391102.2021.1873189},
	author = {Ghosh, Debajeet and Bansode, Sneha and Joshi, Rakesh and Kolte, Baban and Gacche, Rajesh}
}
