Antimicrobial Activity and Conformation of Tachyplesin I and Its Analogs
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概要
- 論文の詳細を見る
We investigated the structure-antimicrobial activity relationship of tachyplesin I (T-I). Even when Lys^1 and Trp^2 were both deleted from the N-terminal end of T-I, the antimicrobial activity against gram-negative bacteria was not decreased. But as Lys^1 and Trp^2 were deleted one by one, the antimicrobial activity against gram-positive bacteria and antiviral activity were gradually decreased. Deletion of two disulfide bridges caused a significant decrease in all activities. The circular dichroism (CD) spectra revealed that the analogs containing the two disulfide bidges took a β-sheet structure and that the analogs without the disulfide bridges took a random coil conformation. These results suggest that the β-sheet structure maintained by two disulfide bridges plays an important role in the antimicrobial activity of T-I.
- 公益社団法人日本薬学会の論文
- 1993-05-15
著者
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藤井 信孝
京都大学薬学部
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村上 司
Osaka City Institute Of Public Health And Environmental Sciences
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玉村 啓和
Faculty of Pharmaceutical Sciences, Kyoto University
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藤井 信孝
Faculty of Pharmaceutical Sciences, Kyoto University
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丹羽 允
Department Of General Education Osaka Institute Of Technology
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藤井 信孝
京大 薬
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Tamamura Hirokazu
Graduate School Of Pharmaceutical Sciences Kyoto University
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玉村 啓和
京都大学大学院薬学研究科
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生駒 理恵
Faculty of Pharmaceutical Sciences, Kyoto University
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舩越 奨
Faculty of Pharmaceutical Sciences, Kyoto University
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舩越 奨
Faculty Of Pharmaceutical Sciences Kyoto University
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生駒 理恵
Faculty Of Pharmaceutical Sciences Kyoto University
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藤井 信孝
京都大学
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