论文部分内容阅读
目的:研究杀菌/渗透增强蛋白(BPI)不同功能区抗菌肽与内毒素(LPS)结合的能力。方法:设计、合成来自杀菌/渗透增强蛋白N端不同功能区的3段抗菌肽,分别为BPI22-36、BPI85-99和BPI147-161,将其固定于CM5蛋白质芯片上,使用表面等离子共振(SPR)仪检测3种抗菌肽与LPS和类脂A(Lipid A)相互作用的情况。结果:3种抗菌肽中,BPI147-161与LPS和Lipid A结合的能力最强,BPI85-99次之,但BPI22-36与其不结合;BPI147-161与Lipid A的亲和常数KA为1.12×106L/mol,相比,多黏菌素B(PMB)的亲和常数KA为5.58×106L/mol。结论:来自杀菌/渗透增强蛋白的抗菌肽BPI147-161能有效地中和内毒素,这可能为败血症休克的治疗提供一种新的策略。
OBJECTIVE: To study the ability of antibacterial peptides to bind endotoxin (LPS) in different functional areas of bactericidal / osmotic enhanced protein (BPI). Methods: Three antibacterial peptides from different functional regions of bactericidal / osmotic enhancing protein N-terminal were designed and synthesized, which were BPI22-36, BPI85-99 and BPI147-161, respectively, which were immobilized on CM5 protein chip and detected by surface plasmon resonance SPR) instrument was used to detect the interaction of three antimicrobial peptides with LPS and Lipid A. Results: Of the three antimicrobial peptides, BPI147-161 had the highest ability to bind to LPS and Lipid A, BPI85-99, but BPI22-36 did not bind to BPI147-161. The affinity constant of BPI147-161 with Lipid A was 1.12 × 106L / mol, the KA of polymyxin B (PMB) was 5.58 × 106L / mol. CONCLUSION: The antibacterial peptide BPI147-161 from bactericidal / osmotic enhancing protein can effectively neutralize endotoxin, which may provide a new strategy for the treatment of septic shock.