Résumé
The principal aims of this study were to identify the composition of salivary pellicles formed on various orthodontic brackets and to obtain a detailed information about the protein adsorption profiles from whole whole saliva and two major glandular salivas. Four different types of orthodontic brackets were used. All were upper bicuspid brackets with a 022 x 028 slot Roth prescription; stainless steel metal, monocrystalline sapphire, polycrystalline alumina, and plastic brackets. Bracket pellicles were formed by the incubation of orthodontic brackets with whole saliva, submandibular-sublingual saliva, and parotid saliva for 2 hours. The bracket pellicles were extracted and confirmed by employing sodium dodecyl sulfate-polyacrylamide gel electrophoresis, Western transfer methods, and immunodetection. The results showed that low-molecular weight salivary mucin, alpha-amylase, secretory IgA (sIgA), acidic proline-rich proteins, and cystatins were attached to all of these brackets regardless of the bracket types. High-molecular weight mucin, which promotes the adhesion of Streptococcus mutans, did not adhere to any orthodontic brackets. Though the same components were detected in all bracket pellicles, however, the gel profiles showed qualitatively and quantitatively different pellicles, according to the origins of saliva and the bracket types. In particular, the binding of sIgA was more prominent in the pellicles from parotid saliva and the binding of cystatins was prominent in the pellicles from the form plastic brackets. This study indicates that numerous salivary proteins adhere to the orthodontic brackets and these salivary proteins adhere selectively according to bracket types and the types of the saliva.