Development of a peptide inhibit oral bacteria related with senile pneumonia

抑制老年肺炎相关口腔细菌肽的研制

• 批准号: 13672145
• 负责人: TANAKA Muneo
• 金额: $ 1.92万
• 依托单位: Osaka University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2001
• 资助国家: 日本
• 起止时间: 2001 至 2002
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-13672145/
• 关键词: statherin; F. nucleatum; bindingsite; Fusobacterium nucleatum; 結合部位

The purpose of this study was to identify the binding sites of salivary, statherin (amino acid residues 1 to 43) to Fusobacterium nucleatum IN our preliminary experiments, we showed that statherin had the strangest binding ability to 125Ilabeled F. nucleatum (125IF. nudeatum) in the various salivary proteins. To determine the binding site of statherin in the binding of 125I-F. nucleatum to stalherincoated hydroxyapatite (sHAP) beads, we performed inhibition assays by using synthetic analogous peptides. As a result, peptide 19-26, 32-39 inhibited F. nudeatum binding to sHAP beads by 77 , 68% respectively. Although, peptide 1-6 , 6-14 did not inhibit. Furthermore, synthetic peptides were prepared by serial deletions of individual residues from N and C termini of peptide GPYQPVPE and QPYQPQYQ. Peptide YQFVPE and PYQPQYQ were found as inhibitory as peptide GPYQPVPE and QPYQPQYQ, respectively. However, further deletions of the residues fiom N and C termini resulted in significant loss of the inhibitory effect. These results suggest that peptide YQPVPE and PYQPQYQ may be the minimal active segment for binding to F. nucleatum which is considered to be related with senile pneumonia

本研究的目的是确定唾液、他汀类药物(氨基酸残基1-43)与核梭杆菌的结合部位。在我们的初步实验中，我们发现他汀类药物与125I标记的核梭杆菌(125IF)具有最奇怪的结合能力。裸藻)在各种唾液蛋白中。确定125I-F结合中施他丁的结合部位。利用人工合成的类似多肽，我们进行了抑制实验。结果表明，19-26、32-39肽对金黄色葡萄球菌与Shap珠子结合的抑制率分别为77%、68%。但多肽1-6、6-14对此无抑制作用。进一步，通过连续缺失GPYQPVPE和QPYQPQYQ的N端和C端的单个残基，制备了合成肽。YQFVPE和PYQPQYQ分别与GPYQPVPE和QPYQPQYQ具有相同的抑制作用。然而，N和C末端残基的进一步缺失导致抑制作用的显著丧失。这些结果表明，YQPVPE和PYQPQYQ可能是与核杆菌结合的最小活性片段，被认为与老年性肺炎有关。