02073nas 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