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首页> 外文期刊>Peptides: An International Journal >Identification of a novel storage glycine-rich peptide from guava (Psidium guajava) seeds with activity against Gram-negative bacteria.
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Identification of a novel storage glycine-rich peptide from guava (Psidium guajava) seeds with activity against Gram-negative bacteria.

机译:从番石榴(Psidium guajava)种子中鉴定出一种新型的富含甘氨酸的肽,该肽具有抗革兰氏阴性细菌的活性。

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Bacterial pathogens cause an expressive negative impact worldwide on human health, with ever increasing treatment costs. A significant rise in resistance to commercial antibiotics has been observed in pathogenic bacteria responsible for urinary and gastro-intestinal infections. Towards the development of novel approaches to control such common infections, a number of defense peptides with antibacterial activities have been characterized. In this report, the peptide Pg-AMP1 was isolated from guava seeds (Psidium guajava) and purified using a Red-Sepharose Cl-6B affinity column followed by a reversed-phase HPLC (Vydac C18-TP). Pg-AMP1 showed no inhibitory activity against fungi, but resulted in a clear growth reduction in Klebsiella sp. and Proteus sp., which are the principal pathogens involved in urinary and gastro-intestinal hospital infections. SDS-PAGE and mass spectrometry (MALDI-ToF) characterized Pg-AMP1 a monomer with a molecular mass of 6029.34Da and small quantities of a homodimer. Amino acid sequencing revealed clear identity to the plant glycine-rich protein family, with Pg-AMP1 the first such protein with activity towards Gram-negative bacteria. Furthermore, Pg-AMP1 showed a 3D structural homology to an enterotoxin from Escherichia coli, and other antibacterial proteins, revealing that it might act by formation of a dimer. Pg-AMP1 shows potential, in a near future, to contribute to development of novel antibiotics from natural sources.
机译:细菌病原体在全球范围内对人类健康造成表达性负面影响,并且治疗成本不断增加。在引起泌尿和胃肠道感染的致病细菌中,已经观察到对商业抗生素的抗性显着提高。为了开发控制这种常见感染的新方法,已经表征了许多具有抗菌活性的防御肽。在此报告中,从番石榴种子(番石榴)中分离了肽Pg-AMP1,并使用Red-Sepharose Cl-6B亲和柱和反相HPLC(Vydac C18-TP)对其进行了纯化。 Pg-AMP1对真菌没有抑制活性,但导致克雷伯菌明显减少。和Proteus sp。,它们是泌尿和胃肠道医院感染的主要病原体。 SDS-PAGE和质谱(MALDI-ToF)表征Pg-AMP1为分子量为6029.34Da的单体,并含有少量的同型二聚体。氨基酸测序揭示了与富含甘氨酸的植物蛋白家族的明确同一性,Pg-AMP1是第一个对革兰氏阴性细菌具有活性的蛋白。此外,Pg-AMP1与来自大肠杆菌的肠毒素和其他抗菌蛋白具有3D结构同源性,表明它可能通过形成二聚体起作用。 Pg-AMP1在不久的将来显示出潜力,可以帮助开发天然来源的新型抗生素。

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