@article{oai:niigata-u.repo.nii.ac.jp:00025382,
 author = {大滝, 俊樹 and 高橋, 信輝 and 武井, 教展 and 谷口, 正之 and 斎藤, 英一},
 journal = {新潟工科大学研究紀要, 新潟工科大学研究紀要},
 month = {Dec},
 note = {Human salivary histidine-rich polypeptides, histatin 1 (38 ammo acids) and histatin 3 (32 aa) are major antimicrobial peptides harboring potent fungicidal activity against Candida albicans. This study was undertaken to examine the activity of four short peptide fragments, histatins 5 (24 aa), 8 (12 aa), 9 (14 aa), and 11 (8 aa), derived from histatin 3 against Porphyromonas gingivalis (penodontal bacteria). By determining the concentration of ATP synthesized by microorganism, histatins 5, 8, 9, and 11 were found to inhibit the growth of P. gingivalis with 50 % inhibitory concentrations (IC_50s) of 33.4, >800, 9.7, and 294.1 μM, respectively. Cytoplasmic membrane depolarization of P. gingivalis by the peptides was elucidated using the membrane-potential-sensitive dye, diSC_3-5. All of the fragments of histatin 3 caused membrane depolarization of 10.4 - 43.9 % at 33.4μM in a good's buffer (5 mM HEPES, pH 7.2, 50 mM glucose) and of 3.5 - 25 % in physiological condition (4 mM NaH_2PO_4/Na_2HP0_4, pH 7.0, 30mM NaCl), respectively. Taken together, it can be concluded that even shorter peptide fragments derived from human histatin 3, show potent antibactencidal activity against P. gingivalis. Thereby, antimicrobial peptides reported here appear to be excellent candidates for oral healthcare products.},
 pages = {9--14},
 title = {ヒト唾液ペプチドの抗菌機能を活用したヘルスケア製品の開発},
 volume = {15},
 year = {2010}
}