人體汗液具有殺菌功效早就為人所知,，但其殺菌原理卻長期未知。對此,，德國研究人員給出了答案,。相關(guān)論文發(fā)表在3月9日的美國《生物化學(xué)期刊》（JBC）上。
德國蒂賓根大學(xué)教授比吉特·席特克和卡爾斯魯厄理工大學(xué)阿納·烏爾里希領(lǐng)導(dǎo)的研究小組發(fā)現(xiàn),，人體皮膚不僅是阻擋異物的天然屏障,，還擁有一套抵抗細(xì)菌、病毒和真菌的化學(xué)防御系統(tǒng),。在這套系統(tǒng)中,，人體汗腺可生產(chǎn)一種DCD多肽，這種通過汗液分布在皮膚表面的多肽不僅可維持皮膚上正常菌群的穩(wěn)定,，還可在致病細(xì)菌的細(xì)胞膜上形成離子通道,，破壞其膜電位,，像抗生素一樣防止皮膚感染。
一般來講,，汗腺會“固定”生產(chǎn)這種殺菌多肽,，以滿足皮膚保護(hù)基本需求，但當(dāng)皮膚受到細(xì)菌感染時,，DCD的產(chǎn)量會隨之增加,。（生物谷Bioon.com）
doi:10.1074/jbc.M111.332270
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Structure-Activity Analysis of the Dermcidin-derived Peptide DCD-1L, an Anionic Antimicrobial Peptide Present in Human Sweat
Maren Paulmann, Thomas Arnold, Dirk Linke, Suat zdirekcan, Annika Kopp, Thomas Gutsmann, Hubert Kalbacher, Ines Wanke, Verena J. Schuenemann, Michael Habeck, Jochen Bürck, Anne S. Ulrich and Birgit Schittek
Dermcidin encodes the anionic amphiphilic peptide DCD-1L, which displays a broad spectrum of antimicrobial activity under conditions resembling those in human sweat. Here, we have investigated its mode of antimicrobial activity. We found that DCD-1L interacts preferentially with negatively charged bacterial phospholipids with a helix axis that is aligned flat on a lipid bilayer surface. Upon interaction with lipid bilayers DCD-1L forms oligomeric complexes that are stabilized by Zn2+. DCD-1L is able to form ion channels in the bacterial membrane, and we propose that Zn2+-induced self-assembly of DCD-1L upon interaction with bacterial lipid bilayers is a prerequisite for ion channel formation. These data allow us for the first time to propose a molecular model for the antimicrobial mechanism of a naturally processed human anionic peptide that is active under the harsh conditions present in human sweat.
