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Title :ヒト唾液短鎖ヒスタチンの口内炎菌(Candida albicans NBRC 1385株)の細胞膜に対する作動性
Title alternative :Action of Human Salivary Short Histatins Against The Cell Membrane of Candida Albicans NBRC 1385
Authors :大滝, 俊樹
笠原, 仁
武井, 教展
谷口, 正之
加藤, 哲男
斎藤, 英一
Publisher :新潟工科大学
Issue Date :Dec-2012
Journal Title :新潟工科大学研究紀要
Volume :17
Start Page :29
End Page :34
ISSN :1342-792X
Abstract :Human saliva contains histains (1 and 3) and their short proteolytic fragments. To study the antifungal mechanism and action against cell membrane of Candida albicans NBRC 1385, we prepared synthetic histatins 5(24 amino acids), 8(12 a.a.), 9(14 a.a.) and 11(8 a.a.). By cell viability assay, half maximal inhibitory concentration (IC50) of histains 5, 8, 9, and 11 was elucidated, respectively, to be 136.7, 251.7, 109.6, and 267.2 μM. When 20 μM melittin was employed as the 100 % control, the percentage of membrane depolarization caused by 20 μM histatins (5, 8, 9, and 11) was determined, respectively, to be 79.9, 16.8, 58.5, and 48.4 % with the membrane potential-sensitive dye diSC_3-5. Using 200 μM melittin as the 100 % control, the percentage of calcein leakage from C. albicans by 200 μM of above histatins was estimated, respectively, to be 65.1, 20.2, 42.8, and 13.2 %. Taken together it may be suggested that histatins attach to the cell membrane of C. albicans via electrostatic interactions. On the membrane surface, the histatins may not only form the pores by placing their hydrophobic part in contact with the hydrophobic core of membrane but also lead to the collapse of the membrane. Based on the ideas, it can be proposed that the interaction between histatins and phospholipid of cell membrane mediates C. albicans-killing process.
Keywords :Human saliva
antimicrobial peptide
proteolysis
short peptides
histatin 3
candida albicans
Type Local :Departmental Bulletin Paper
Language :jpn
URI :http://hdl.handle.net/10623/38605
Appears in Collections:01 新潟工科大学研究紀要 = Bulletin of Niigata Institute of Technology

Please use this identifier to cite or link to this item: http://hdl.handle.net/10623/38605

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