02058nas a2200229   4500008004100000022001400041245012000055210006900175260010600244300001200350490000700362520113700369653001301506653004101519653002801560653003201588100001901620700002001639700002401659700002101683856012401704       2005                        eng d  a0022-191000aCharacterization of two midgut proteinases of helicoverpa armigera and their interaction with proteinase inhibitors0 aCharacterization of two midgut proteinases of helicoverpa armige  aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcMAY  a513-5220 v513 a<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>10aelastase10aHelicoverpa armigera gut proteinases10ainsect-resistant plants10aplant proteinase inhibitors1 aTelang, M., A.1 aGiri, Ashok, P.1 aSainani, Mohini, N.1 aGupta, Vidya, S.  uhttps://library.ncl.res.in/content/characterization-two-midgut-proteinases-helicoverpa-armigera-and-their-interaction-002073nas a2200253   4500008004100000022001400041245007300055210006900128260000800197300001400205490000700219520130800226653001401534653001301548653002201561653002601583653001501609100002001624700001901644700001801663700001701681700001901698856010201717       2022                        eng d  a0739-110200aMolecular elucidation of pancreatic elastase inhibition by baicalein0 aMolecular elucidation of pancreatic elastase inhibition by baica  cJUL  a5759-57680 v403 a<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>
10aBaicalein10aelastase10aEnzyme inhibition10amolecular interaction10asivelestat1 aGhosh, Debajeet1 aBansode, Sneha1 aJoshi, Rakesh1 aKolte, Baban1 aGacche, Rajesh  uhttps://library.ncl.res.in/content/molecular-elucidation-pancreatic-elastase-inhibition-baicalein