人ⅡA型磷脂酶A衍生多肽M17杀菌作用的研究

淳于柳爽; 梁宁生

doi:10.11653/syfj2013200216

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人ⅡA型磷脂酶A衍生多肽M17杀菌作用的研究

更新时间：2024-01-04

- 人ⅡA型磷脂酶A衍生多肽M17杀菌作用的研究
- Study on Bactericidal Activity of the Polypeptide M17 Derived from Human Group ⅡA Phospholipase A
- 中国实验方剂学杂志 2013年19卷第20期页码：216-219
- 作者机构：
- 作者简介：
- 基金信息：
  
  广西医药卫生重点科研课题( 重2011075);广西自然科学基金项目(2010GXNSFA013246)
- DOI：10.11653/syfj2013200216
  中图分类号：
- 纸质出版日期：2013
- 稿件说明：
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淳于柳爽, 梁宁生. 人ⅡA型磷脂酶A衍生多肽M17杀菌作用的研究[J]. 中国实验方剂学杂志, 2013,19(20):216-219.

CHUN YU Liu-shuang, LIANG Ning-sheng. Study on Bactericidal Activity of the Polypeptide M17 Derived from Human Group ⅡA Phospholipase A[J]. Chinese journal of experimental traditional medical formulae, 2013, 19(20): 216-219.
淳于柳爽, 梁宁生. 人ⅡA型磷脂酶A衍生多肽M17杀菌作用的研究[J]. 中国实验方剂学杂志, 2013,19(20):216-219. DOI： 10.11653/syfj2013200216.

CHUN YU Liu-shuang, LIANG Ning-sheng. Study on Bactericidal Activity of the Polypeptide M17 Derived from Human Group ⅡA Phospholipase A[J]. Chinese journal of experimental traditional medical formulae, 2013, 19(20): 216-219. DOI： 10.11653/syfj2013200216.

摘要

目的: 研究和比较人ⅡA型磷脂酶A2(phospholipase A2

PLA2)衍生多肽M17

P26和N1-11对不同细菌在体外的杀菌效应。方法: 根据人ⅡA型PLA2氨基酸顺序分别设计合成3个肽分子M17(p51-67)

P26(p99-124)

N1-11(p1-11)。采用琼脂铺板计数法测定杀菌活性

将不同浓度衍生肽分别与革兰阳性菌(G+)金黄色葡萄球菌、枯草杆菌、屎肠球菌和革兰阴性菌(G-)大肠杆菌、绿脓杆菌、鲍曼不动杆菌在37℃孵育2.5 h

然后铺板并置于37℃恒温箱培养18~24 h

记录每一琼脂板上的菌落数(CFU)

并计算多肽作用后的杀菌率。结果: ⅡA型PLA2M17对枯草杆菌、金黄色葡萄球菌、屎肠球菌的杀菌回归方程分别为:Y=1.464X+3.795(ED50 6.65 mg·L-1)

Y=1.152X+3.419(ED50 23.57 mg·L-1)

Y 0.836X+3.832 (ED50 24.95 mg·L-1);对大肠杆菌、鲍曼不动杆菌、绿脓杆菌的杀菌回归方程分别为:Y=0.877X+4.054(ED50 12.00 mg·L-1)

Y=1.094X+3.371(ED50 30.83 mg·L-1)

Y=1.027X+3.626(ED50 21.77 mg·L-1);M17肽分子对G+菌与G-菌均有较强的杀菌活性。P26和N1-11对金黄色葡萄球菌的杀菌回归曲方程分别为:Y=0.915X+2.766(ED50 276.39 mg·L-1)

Y=1.389X+1.668(ED50 250.52 mg·L-1)

P26和 N1-11对大肠杆菌的杀菌回归方程为:Y=1.327X+1.437(ED50 484.18 mg·L-1)

Y=0.881X+2.903(ED50 240.02 mg·L-1);N1-11和P26对G+菌有较强的杀菌活性

但对G-菌杀菌活性较弱。M17肽分子对金黄色葡萄球菌的杀菌活性强于P26及N1-11

M17肽分子对大肠杆菌的杀菌活性明显强于P26及N1-11。结论: 衍生自人ⅡA型PLA2保守区域17个氨基酸残基的肽M17对G+菌和G-菌均有较强的杀菌活性

这可能与M17肽分子更易于与细菌结合并发挥作用有关。

Abstract

Objective: To study and compare the bactericidal activity of the polypeptide M17

P26 and N1-11 which derives from hunman group ⅡA phospholipase A2 (PLA2

phospholipase A2) in vitro. Method: Peptide M 17(p51-67)

P26 (p99-124)

N1– 11 (p1-11) were synthesized according to the sequence of human GroupⅡA PLA2 amino acid. Six species of bacterial

Gram positive(G+) Staphy 1ococcus aureus

Bacillus subtilis

Enterococcus faecium

Gram negative(G-) Escherichia coli

Acinetobacter baumannii

Bacillus pyocyaneus

were incubated with different concentration of polypeptides at 37℃ for 2.5 hours in a water bath respectively. Then the reaction solution was diluted and agar plates were poured. After 18-24 hours incubation in the thermostated container at 37℃.The colony formed units were counted and the bactericida1 rates were calculated. Result: Regression equation of PLA2M17 bactericidal activity on the G+ bacteria(lococcus aureus

Bacillus subtilis

Enterococcus faecium) were Y=1.464X+3.795(ED50 6.65 mg·L-1)

Y=1.152X+3.419(ED50 23.57 mg·L-1)

Y=0.836X+3.832 (ED50 24.95 mg·L-1). Regression equation of M17 bactericidal activity on the G-bacteria (E. coli

A. baumannii

B. pyocyaneus)were Y=0.877X+4.054(ED50 12.00 mg·L-1)

Y=1.094X+3.371(ED50 30.83 mg·L-1)

Y=1.027X+3.626(ED50 21.77 mg·L-1). PLA2M17 possessed potent bactericidal activity on the G+ bacteria and G-bacteria.Regression equation of N1-11 and P26 bactericidal activity on B. subtilis were Y=0.915X+2.766(ED50 276.39 mg·L-1)

Y=1.389X+1.668(ED50 250.52 mg·L-1). Regression equation of N1-11 and P26 bactericidal activity on E. coli were Y=1.327X+1.437(ED50 484.18 mg·L-1)

Y=0.881X+2.903(ED50 240.02 mg·L-1).N1-11 and P26 possessed strong bactericidal activity of G+ bacteria

but weaker activity of G- bacteria. M17 possessed stronger bactericidal activity than N1-11 and P26 on B. subtilis and E. coli. Conclusion: Peptide M17 derived from human Ⅱ type A PLA2 highly conserve region possesses a strong bactericidal activity

this may be related to the M17 peptide molecules more easily binding to bacteria.

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