The previous grant period established the structure-function relationships whereby salivary statherin and mucins take part in different hard tissue lubrication regimes. The renewal application proposes to define further and then enhance the physicochemical properties of lubricants at the enamel interface. The identification of new high lubricity amphipaths may lead to treatment modalities for the clinical manifestations of dental abrasion and attrition. The immediate objectives are the establishment of the complete paradigm of the boundary lubrication of enamel. We propose to study small model amphipathic compounds which will then assist us in the design of more complex macromolecules including statherin mutants developed in Subproject I.B. Different modes of delivery of lubricant molecules to enamel surface will be explored including: 1) model compounds in aqueous solutions; 2) insoluble films deposited on enamel from nonaqueous solvents; and 3) slow release delivery from dental material such as composite resins. These formats cover the spectrum of clinical possibilities and should lead to real systems capable of reducing interdental friction coefficient below 0.1 for prolonged periods of time. Investigations on natural salivas, purified mucins, mucin derivatives, and mucin/albumin complexes will also include water evaporative loss which is controlled by colligative properties and the rheological characteristics. These studies may elucidate the role of mucin solvation in the thick film component of thin film lubrication. Collectively, these studies will set new criteria for the performance of salivary substitutes which will include lubricity, water retention and flow characteristics, and in this way to enhance or improve upon the protective properties of saliva.

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Specialized Center (P50)
Project #
2P50DE008240-06
Application #
3839369
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
6
Fiscal Year
1992
Total Cost
Indirect Cost
Name
State University of New York at Buffalo
Department
Type
DUNS #
038633251
City
Buffalo
State
NY
Country
United States
Zip Code
14260
Ohkusa, Toshifumi; Yoshida, Tsutomu; Sato, Nobuhiro et al. (2009) Commensal bacteria can enter colonic epithelial cells and induce proinflammatory cytokine secretion: a possible pathogenic mechanism of ulcerative colitis. J Med Microbiol 58:535-45
Sojar, Hakimuddin T; Genco, Robert J (2005) Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds to Porphyromonas gingivalis fimbriae. FEMS Immunol Med Microbiol 45:25-30
Satyanarayana, J; Gururaja, T L; Narasimhamurthy, S et al. (2001) Synthesis and conformational features of human salivary mucin C-terminal derived peptide epitope carrying Thomsen-Friedenreich antigen: implications for its role in self-association. Biopolymers 58:500-10
Narasimhamurthy, S; Naganagowda, G A; Janagani, S et al. (2000) Solution structure of O-glycosylated C-terminal leucine zipper domain of human salivary mucin (MUC7). J Biomol Struct Dyn 18:145-54
Tseng, C C; Miyamoto, M; Ramalingam, K et al. (1999) The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase. Arch Oral Biol 44:119-27
Naganagowda, G A; Gururaja, T L; Satyanarayana, J et al. (1999) NMR analysis of human salivary mucin (MUC7) derived O-linked model glycopeptides: comparison of structural features and carbohydrate-peptide interactions. J Pept Res 54:290-310
Sojar, H T; Han, Y; Hamada, N et al. (1999) Role of the amino-terminal region of Porphyromonas gingivalis fimbriae in adherence to epithelial cells. Infect Immun 67:6173-6
Mettath, S; Munson, B R; Pandey, R K (1999) DNA interaction and photocleavage properties of porphyrins containing cationic substituents at the peripheral position. Bioconjug Chem 10:94-102
Gururaja, T L; Levine, J H; Tran, D T et al. (1999) Candidacidal activity prompted by N-terminus histatin-like domain of human salivary mucin (MUC7)1. Biochim Biophys Acta 1431:107-19
Satyanarayana, J; Gururaja, T L; Naganagowda, G A et al. (1998) A concise methodology for the stereoselective synthesis of O-glycosylated amino acid building blocks: complete 1H NMR assignments and their application in solid-phase glycopeptide synthesis. J Pept Res 52:165-79

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