Sat. Apr 20th, 2024

L coordination bond (black line), and two salt bridge (red-violet line
L coordination bond (black line), and two salt bridge (red-violet line) formation within the catalytic pocket of mh-Tyr protein against co-crystallized reference ligand (Fig. S5). These CysLT2 supplier results assistance the regarded docking grid and other parameters as excellent for the analysis of selected flavonoids with mh-Tyr. Following, the XP docking of selected flavonoids yields the highest binding affinities in between – 9.346 to – 5.301 kcal/mol against the ARB inhibitor (- 5.795 kcal/mol) with mh-Tyr (Table S1, Fig. 2). As a result, the bestdocked poses of mh-Tyr with respective compounds at highest adverse docking scores had been chosen for additional intermolecular interaction analysis. As depicted in Fig. two, all of the functional groups on A, B, and C-ring of 3 flavonoids, viz. C3G, EC, and CH, showed differential interactions with the catalytic center of mh-Tyr containing binuclear copper ions (CuA400 and CuB401) by comparison towards the ARB inhibitor. Herein, mh-Tyr-C3G docked complex was noted for the highest docking score of -9.346 kcal/mol and exhibited four hydrogens (H)-bonds at Gly281 (C=OH, OH of Glycosyl-ring in C3G: two.03 , COX-2 review Arg268 (N-HO, OH of Glycosyl-ring in C3G: 2.06 , and Glu322 (2; C=OH, OH of B-ring in C3G:1.97 and C=OH, OH of B-ring in C3G: two.20 residues, and interactions using the binuclear copper ions (Cu400 and Cu401) through salt bridge formation at deprotonated hydroxyl group inside the A-ring of C3G. In addition, hydrophobic (Val248, Phe264, and Val283), polar (His61, His85, Hie244: histidine neutral -protonated, His259, Asn260, His263, and Ser282), constructive (Arg268), negative (Glu322), glycine (Gly281), and – (formation via A-ring in C3G with His85 and His263 residues) intermolecular contacts had been also noted inside the mh-Tyr-C3G docked complicated (Fig. 2a,b). Likewise, molecular docking of EC using the mh-Tyr revealed -6.595 kcal/mol docking power, contributed by metal coordination bond (Cu400) formation at deprotonated hydroxyl group in B-ring of EC in addition to other intermolecular interactions, like hydrophobic (Phe90, Cys83, Val248, Phe264, Met280, Val283, Ala286, and Phe292), polar (His61, His85, His244, His259, Asn260, His263, and Ser282), glycine (Gly281), and – bond formation by way of B-ring in EC (His85, His259, and His263) interactions (Fig. 2c,d). Similarly, the mh-Tyr-CH docked complicated was marked for – five.301 kcal/mol and formed two hydrogen bonds with Asn260 (C=OH, OH of C-ring in CH: 2.02 and Gly281 (C=OH, OH of A-ring in CH: two.02 residues. Furthermore, salt bridge (Cu400 and Cu401), metal coordination bond (Cu400 and Cu401), hydrophobic (Phe90, Val248, Phe264, Pro277, Met280, Val283, Ala286, and Phe292), polar (His61, His85, His94, His244, His259, Asn260, His263, Ser282, and His296), good (Arg268), unfavorable (Glu256), and Glycine (Gly281), bond formation by way of B-ring (His259 and His263) and A-ring (Phe264), and -cation bond formation by way of A-ring (Arg268) contacts were also recorded in the mh-Tyr-CH docked complex (Fig. 2e,f). On the other hand, molecular docking of ARB inhibitor in the active pocket of the mh-Tyr showed a fairly much less unfavorable docking score (- 5.795 kcal/mol) and contributed by single H-bond at Asn260 (C=OH, OH of Glycosyl-ring in ARB: 1.73 , hydrophobic (Phe90, Val248, Met257, Phe264, Met280, Val283, Ala286, and Phe292), polar (His61, His85, Hie244: histidine neutral -protonated, His259, Asn260, His263, and Ser282), adverse (Glu256), glycine (Gly281), and – bond at phenol-ring of ARB (Phe264) interactions (Fig. 2g,h). Of note, all.