α-Mangostin Disrupts the Development of Streptococcus mutans Biofilms and Facilitates Its Mechanical Removal
Figure 5
Snapshot of glucosyltransferase interaction with αMG compound and influence of 150 µM αMG on the activities of GtfB and GtfC.
Panel A depicts the ribbon model of glucosyltransferase C (brown) docking α-mangostin (blue) using HEX-docking software Amino acids, such as Trp 517, Glu 515, Asp 588 and Asn 481 are interacting in the glucosyl binding site. Panel B depicts the surface model of glucosyltransferase C docking α-mangostin (red) and acarbose (purple) using HEX-docking software. Panel C depicts the glucosyltransferase B 3D ligand-binding site predicted model using Phyre Server. Panel D depicts Gtf activity of S. mutans cells when treated with αMG. The percentage of inhibition was calculated setting the vehicle control to 100% Gtf activity. Data are expressed as the mean ± one standard deviation. Values are significantly different from that for the vehicle control (n = 12; P<0.05, pair-wise comparison using Student’s t test).