ABSTRACT
AIM: The aim of this study was to assess the effectiveness of two herbal mouthwashes in comparison with Chlorhexidine mouthwash on gingivitis. MATERIALS AND METHODS: This is a triple-blind randomized controlled clinical trial, where in 60 patients were randomly allocated into three study groups: Triphala mouthwash (Group A), Aloe vera mouthwash (Group B), and Chlorhexidine mouthwash (Group C). All groups were treated with scaling and asked to rinse with respective mouthwashes twice daily for 1 month. Clinical parameters such as plaque index (PI), gingival index (GI), and bleeding index (BI) were recorded at baseline, 15 days, and 30 days, respectively. RESULTS: Our results suggested that Triphala group effectively demonstrated a higher reduction in GI and BI index scores compared to A. vera group (P ≤ 0.005) and the effect is equivocal to the reduction seen with Chlorhexidine group. However, no statistically significant difference was observed between the mouthwashes in reduction of PI scores (P > 0.005). CONCLUSION: The results of our study evidenced Triphala to be superior in the reduction of plaque, gingival inflammation, and bleeding compared to that of A. vera. However, the results of our study also indicated that Triphala was as effective as chlorhexidine mouthwash in its ability in reducing plaque accumulation, gingival inflammation, and bleeding. Furthermore, Triphala is relatively free of side effects compared to that of chlorhexidine.
ABSTRACT
Staphylococcus aureus is an opportunistic pathogen that rapidly acquires resistance to frontline antibiotics. The characterization of novel protein targets from this bacterium is thus an important step towards future therapeutic strategies. Here, the crystal structure of an amidohydrolase, SACOL0085, from S. aureus COL is described. SACOL0085 is a member of the M20D family of peptidases. Unlike other M20D peptidases, which are either monomers or dimers, SACOL0085 adopts a butterfly-shaped homotetrameric arrangement with extensive intersubunit interactions. Each subunit of SACOL0085 contains two Mn(2+) ions at the active site. A conserved cysteine residue at the active site distinguishes M20D peptidases from other M20 family members. This cysteine, Cys103, serves as bidentate ligand coordinating both Mn(2+) ions in SACOL0085.
