Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Avenida Universidad, 2001, Colonia Chamilpa, Apartado Postal 510-3, Cuernavaca, Morelos 62210, Mexico.
Peptides. 2012 Apr;34(2):290-5. doi: 10.1016/j.peptides.2012.02.002. Epub 2012 Feb 10.
From the cDNA libraries made from the venom glands of two scorpions belonging to the Vaejovidae family, four different putative non disulfide-bridged antimicrobial peptides were identified: VmCT1 and VmCT2 from Vaejovis mexicanus smithi plus VsCT1 and VsCT2 from Vaejovis subcristatus. These short peptides (with only 13 amino acid residues each) share important amino acid sequence similarities among themselves and with other reported antimicrobial peptides, but their biological activities vary dramatically. This communication reports the cloning, chemical synthesis and characterization of these peptides. Two peptides, VmCT1 and VmCT2 showed broad-spectrum antibacterial activity with minimum inhibitory concentrations MICs in the range of 5-25 μM and 10-20 μM respectively, whereas their hemolytic activity at these concentrations was low. Structure-function relationships that might determine the differences in activities are discussed.
从属于 Vaejovidae 科的两只蝎子的毒腺 cDNA 文库中,鉴定出四种不同的假定非二硫键桥连的抗菌肽:来自 Vaejovis mexicanus smithi 的 VmCT1 和 VmCT2 以及来自 Vaejovis subcristatus 的 VsCT1 和 VsCT2。这些短肽(每个肽只有 13 个氨基酸残基)在彼此之间以及与其他报道的抗菌肽之间具有重要的氨基酸序列相似性,但它们的生物学活性差异很大。本通讯报告了这些肽的克隆、化学合成和特性。两种肽,VmCT1 和 VmCT2 显示出广谱抗菌活性,最低抑菌浓度(MIC)范围分别为 5-25 μM 和 10-20 μM,而在这些浓度下的溶血活性较低。讨论了可能决定活性差异的结构-功能关系。