SALIVA-GLUCOSYLTRANSFERASE INTERACTIONS ON SURFACES

具有酶活性的葡糖基转移酶与 获得性釉质膜的宿主衍生成分，以及 GTF活性的产物，可能在形成和 牙菌斑的成熟。 葡萄糖基转移酶优选吸附至 唾液包被的羟基磷灰石（sHA）在体外和体内， 大大提高了葡聚糖的合成能力。 研究结果， 我们的实验室表明，葡萄糖基转移酶表达催化 在较宽的pH（4.5-7.5）和温度范围内的活性， 在溶液中的酶。 原位合成的葡聚糖强烈粘附 表面，并为变形链球菌提供结合位点 和远缘链球菌。 这些数据的临床相关性是 通过观察到没有作用的氨基醇 对酶在溶液中的吸附有效地抑制了酶， 面 为了进一步探索这些重要现象，我们建议 确定是否由S.变聚糖（GTF-1， GTF-SI、GTF-S）在它们粘附sHA的能力上不同。 我们将使用 从已经克隆了所述基因的生物体制备的酶， 从而使酶的纯化不那么困难。 在 此外，我们将利用凝胶电泳和抗体， 特别是唾液中与GTF相互作用的成分。 通过 通过交联的方法，我们将尝试鉴定GTF中的肽 与唾液成分发生反应， 为了生物学地制备可用于与GTF竞争的肽， sHA上的结合位点，从而提供对性质的额外了解 这些相互作用，并可能指出发展的道路， 抗牙斑剂。 我们将研究其结构、分子量和 原位形成的葡聚糖的溶解度。 这些信息可能会使它 可以设计出与S竞争的分子。变形菌和 某些放线菌在葡聚糖覆盖的表膜上生长。

The interaction of enzymatically active glucosyltransferase with host-derived constituents of the acquired enamel pellicle, as well as the products of GTF activity, may play a profound role in the formation and maturation of dental plaque. Glucosyltransferase adsorbs preferably to salivary-coated hydroxyapatite (sHA) in vitro and in vivo and expresses greatly enhanced glucan synthesizing ability. Results from studies in our laboratory indicate that glucosyltransferase expresses catalytic activity over a broad range of pH (4.5-7.5) and temperature when compared with the enzyme in solution. Glucan synthesized in situ adheres strongly to the sHA surface and provides binding sites for Streptococcus mutans and Streptococcus sobrinus. The clinical relevance of these data is enhanced by the observation that an amino alcohol which is without effect on the enzyme in solution effectively inhibits the enzyme adsorbed to a surface. To explore these important phenomena further, we propose to determine whether the different GTF enzymes produced by S. mutans (GTF-I, GTF-SI, GTF-S) differ in their ability to adhere to sHA. We will use enzymes prepared from an organism into which the genes have been cloned, thereby rendering purification of the enzymes less difficult. In addition, using gel electrophoresis and antibodies, we will examine specifically the constituents in saliva with which the GTF interacts. By means of cross-linking, we will attempt to identify the peptides in GTF that react with salivary constituents and use the information generated to biologically prepare peptides that can be used to compete with GTF for binding sites on sHA, thereby providing additional insight to the nature of these interactions and possibly pointing the way to development of antiplaque agents. We will examine the structure, molecular weight, and solubility of the glucans formed in situ. Such information may make it possible to design molecules which will compete with S. mutans and certain actinomyces for sites on glucan-coated pellicle.