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离子梯度调节人类calprotectin的亲和力和抗菌活性
Megan Brunjes Brophy1, Joshua A Hayden, Elizabeth M Nolan
1Department of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Journal of the American Chemical Society
|October 23, 2012
概括
蛋白 (CP) 是一种抗微生物蛋白质,它与结合. 它的结合亲和力由增强,使其能够抑制细胞外环境中的细菌生长.
科学领域:
- 生物化学 生物化学
- 这是一种金属蛋白质.
- 抗微生物机制的抗微生物机制
背景情况:
- 蛋白 (CP) 是一种来自中性粒细胞的抗微生物蛋白.
- CP 封存必要的金属营养物质,以抑制微生物生长.
- 了解CP的金属结合特性对于其抗菌功能至关重要.
研究的目的:
- 为了界定calprotectin的结合特性.
- 为了确定CP.内特定的金属结合点.
- 阐明在CP的结合和抗菌活性中的作用.
主要方法:
- 使用Co(II) 作为探针 (光学吸收,EPR) 的光谱研究.
- 用竞争定位进行热力学金属结合研究.
- 在体外抗菌活性测定.
主要成果:
- 在CP中确定了His(3) Asp和His(4) 结合位的独特光谱特征.
- 确定了2:1Zn(II):CP静脉测量,两个位点都与Zn(II) 协调.
- 证明了CP的亲和力取决于,在Ca存在时显著增加.
结论:
- 卡尔蛋白蛋白利用特定的富含His的位点来结合,其亲和力由调节.
- 生理学梯度可能调节CP的强大的细胞外化.
- CP需要金属结合点和来有效抑制阳性和阴性细菌.
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