This work was supported by a grant from Tianjin Science and Technology Development Project (003119311).
LL-37是迄今在人体中发现的抗菌肽cathelicidin家族中的唯一成员,也是人体内唯一的双亲性α螺旋结构的抗菌肽. LL-37在人体的血液细胞和上皮细胞中广泛分布,具有广谱抗菌作用.抗菌活性依赖其螺旋构象的形成,通过“地毯样”机制杀灭细菌. LL-37有中和内毒素的作用,能与LPS和CD14结合,中和LPS的生物活性,还能利用formyl peptide receptor-like 1 (FPRL1) 作为受体介导趋化作用,招募免疫细胞到感染部位,清除病原物. 很多感染性疾病都与LL-37低表达或功能失活有关. LL-37是一种多功能的抗菌肽,有开发成为具有抗菌和增强免疫力双重作用药物的潜力.
The antimicrobial peptide LL-37 belongs to the cathelicidin family and is the unique amphipathic α-helical peptide identified in humans up to date. LL-37 is not only a major protein of blood cells, but is also present in epithelial cells. This peptide has a broad spectrum of antimicrobial activity, which kills bacteria by disrupting membrane according to the “carpet like” mechanism. LL-37 possesses the ability to bind lipopolysaccharide(LPS) and neutralizes its biological activity via its binding activities for LPS and CD14. In addition, LL-37 acts as a chemoattractant to recruit immune cells to site of infection by binding to formyl peptide receptor-like 1 FPRL1. Taken together, LL-37 is a multifunctional modulator of innate immune responses and might have the therapeutic potential for the treatment of bacterial infection and immunocompromise.
杨应华,马文儒,郑国光,吴克复.人源抗菌肽LL-37[J].生物化学与生物物理进展,2003,30(6):847-851
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