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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, \u003e800, 9.7, and 294.1 \u03bcM, 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 33.4\u03bcM in a good\u0027s 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.", "subitem_description_type": "Abstract"}]}, "item_7_full_name_3": {"attribute_name": "\u8457\u8005\u5225\u540d", "attribute_value_mlt": [{"nameIdentifiers": [{"nameIdentifier": "149571", "nameIdentifierScheme": "WEKO"}], "names": [{"name": "Ohtaki, Toshiki"}]}, {"nameIdentifiers": [{"nameIdentifier": "149572", "nameIdentifierScheme": "WEKO"}], "names": [{"name": "Takahashi, Nobuteru"}]}, {"nameIdentifiers": [{"nameIdentifier": "149573", "nameIdentifierScheme": "WEKO"}], "names": [{"name": "Takei, Norinobu"}]}, {"nameIdentifiers": [{"nameIdentifier": "149574", "nameIdentifierScheme": "WEKO"}], "names": [{"name": "Taniguchi, Masayuki"}]}, {"nameIdentifiers": [{"nameIdentifier": "149575", "nameIdentifierScheme": "WEKO"}], "names": [{"name": "Saitoh, Eiichi"}]}]}, "item_7_publisher_7": {"attribute_name": "\u51fa\u7248\u8005", "attribute_value_mlt": [{"subitem_publisher": 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