Frank G. Oppenheim, DMD, PhD
|Institution||Boston University Henry M. Goldman School of Dental Medicine|
|Department||Molecular & Cell Biology|
|Address||700 Albany St Ctr for Adv Biomed Res|
Boston MA 02118
|Institution||Boston Medical Center|
The work of my laboratory focuses on the elucidation of structure and function of salivary proteins, which play important role in host defense mechanisms. Structural analysis, peptide biomimetics employing solid phase peptide synthesis and recombinant expression methods are being used in the identification of functional domains within proteins. Functional investigations comprise mechanisms related to anti-bacterial, anti-fungal and mineral homeostasis. Emphasis on these processes is aimed at understanding the basic physiology of hard and soft tissue protection in the oral environment. Proteins such as the histatins, the proline-rich proteins and statherin are examples of proteins unique to the oral cavity. For example, the discovery of the histatin protein family showed that these small basic proteins are rich in histidine, exhibit anti-microbial properties, contain specific functional domains, and are able to kill yeasts by entering cells and target mitochondria. The mechanisms of cell death is being studied. and it has been shown that the killing effect of histatins is related to the inhibition of the respiratory chain leading to the formation reactive oxygen radicals. Other studies in progress comprise the identification and characterization of salivary protein which show selective adsorption to hydroxyapaptite forming a unique protein film on the mineral surfaces of teeth. This protein film determines de- and re-mineralization processes and dictates the early events of microbial colonization.. These studies include biophysical techniques such as NMR and mass spectrometry. Approaches of proteomics are being used to characterize proteins and peptides formed on mineral surfaces in vivo.