Development of a peptide inhibit oral bacteria related with senile pneumonia

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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