Biphenomycin A

Introduction: The adhesives used to bond orthodontic retentions are low-loaded composite resins with a resinous matrix containing bisphenol A diglycidyl ether dimethacrylate synthesized from bisphenol A (BPA), fluidizers such as triethylene glycol dimethacrylate (TEGDMA) and hydrophilic polymers such as hydroxyethylmethacrylate. BPA disrupts the endocrine balance, and TEGDMA has high risks for human health: eg, allergies and cytotoxicity. The aim of this study was to evaluate in vitro the release of monomers from orthodontic bonded retentions. Methods: A reproducible model of bonded retentions was carried out using calibrated molds. We analyzed the release of monomers by gas phase chromatography coupled with mass spectrometry. Results: This model allowed us to qualitatively and quantitatively evaluate the in-vitro release of monomers from orthodontic adhesives. The quantitative and qualitative analyses showed no BPA release above the 0.02 ppm detection limit. A greater release of TEGDMA was observed with Transbond LR (31.7 μg/mL) than with Transbond XT (13.12 μg/mL) (both, 3M Unitek, Monrovia, Calif). Other toxic components (iodobenzene, iodobiphenyl, triphenyl stibine, and so on) were also identified. Conclusions: Toxic and carcinogenic molecules not mentioned in the material safety data sheets were identified.

Production of biphenomycin A by Streptomyces griseorubiginosus 43708 was stimulated by a mixed culture with a partner strain, Pseudomonas maltophilia 1928. This stimulatory effect on biphenomycin A accumulation by the mixed culture was caused by the enzyme activity which strain 1928 possessed. It is suggested that in a mixed culture strain 43708 produces a precursor of biphenomycin A in culture broth and that strain 1928 converts the precursor to biphenomycin A.

A precursor of biphenomycin A in mixed culture of Streptomyces griseorubiginosus No. 43708 with Pseudomonas maltophilia No. 1928 was isolated and characterized. The structure of the precursor, designated biphenomycin C was determined to be a peptide which is composed of biphenomycin A and arginylserine residue (Fig. 1), on the basis of chemical and spectroscopic evidence.