详细信息
黄粉虫幼虫小分子量抗菌肽的分离纯化 被引量:3
Isolation and purification of small antimicrobial peptide from larvae of mealworm,Tenebrio molitor
文献类型:期刊文献
中文题名:黄粉虫幼虫小分子量抗菌肽的分离纯化
英文题名:Isolation and purification of small antimicrobial peptide from larvae of mealworm,Tenebrio molitor
作者:孙龙[1] 冯颖[1] 何钊[1] 陈智勇[1] 赵敏[1]
第一作者:孙龙
机构:[1]中国林业科学研究院资源昆虫研究所国家林业局资源昆虫培育与利用重点实验室,昆明650224
年份:2012
卷号:49
期号:3
起止页码:686-692
中文期刊名:应用昆虫学报
外文期刊名:Chinese Journal of Applied Entomology
收录:CSTPCD;;北大核心:【北大核心2011】;CSCD:【CSCD2011_2012】;
基金:国家林业局基地建设项目(1691116001242);国家林业局引进国际先进林业科学技术项目(20064116);中央级公益性科研院所基本科研业务费专项项目(riricaf2011001M)
语种:中文
中文关键词:黄粉虫;抗菌肽;凝胶色谱;质谱
外文关键词:Tenebrio molitor, antimicrobial peptide, gel chromatography, mass spectrometry
分类号:Q966
摘要:昆虫抗菌肽具有良好的抑菌效果,有望开发成新一代抗生素。本文以金黄色葡萄球菌和大肠杆菌混合液作为诱导源,采用针刺法使黄粉虫Tenebrio molitor L.幼虫感染微生物产生抗菌肽,并对抗菌肽进行了提取、色谱分离纯化及抑菌活性检测。结果显示,诱导组和对照组的三氟乙酸粗提物无抑菌活性;经SephadexG50、SuperdexPeptide凝胶色谱分离后,从诱导组和对照组均可获得对革兰氏阳性菌金黄色葡萄球菌、枯草芽孢杆菌有抑菌作用的组分,而且诱导组活性明显高于对照组;通过Resource 15RPC反相色谱分离纯化,从诱导组获得一具有明显抑制革兰氏阳性菌的组分,质谱检测该组分为混合肽,主要由分子量为1 876.21 u、1 904.21 u的小肽组成,可能是一种比Thanatin分子量更低的昆虫抗菌肽。
Antimicrobial peptides (AMPs) are so effective against bacteria that they are expected to become the new antibiotics. We induced mealworm, Tenebrio molitor L, , larvae to produce AMPs by pricking their abdomens with a stainless needle that had been dipped in a suspension of living Escherichia coli and Staphylococcus aureus. AMPs were then isolated and purified by methods including 0.1% trifluoroacetic acid ( v: v) extraction, gel filtration chromatography on Sephadex G - 50 and Superdex Peptide, and reverse phase high - performance liquid chromatography ( RP - HPLC). Eventually, a fraction was obtained from the induced group with strong anti - S. aureus and anti - Bacillus subtilis activities. The analysis of matrix - assisted laser desorption ionization time - of - flight mass spectrometry ( MALDI - TOF MS) indicated that the fraction was composed of two small peptides with molecular masses of 1 876.21 u and 1 904.21 u respectively. This suggests that these peptides are insect AMPs of a lower molecular weight than Thanatin.
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