Phylloseptin-PBa--A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity.

Phylloseptin-PBa--A Novel Broad-Spectrum Antimicrobial Peptide from the Skin Secretion of the Peruvian Purple-Sided Leaf Frog (Phyllomedusa Baltea) Which Exhibits Cancer Cell Cytotoxicity.
复制标题

DOI:
10.3390/toxins7124878
复制
发表时间:
2015-12-01
期刊:
影响因子:
4.2
通讯作者:
Shaw C
Shaw C
中科院分区:
医学2区
文献类型:
--
作者:
Wan Y;Ma C;Zhou M;Xi X;Li L;Wu D;Wang L;Lin C;Lopez JC;Chen T;Shaw C

文献摘要

被引文献

相似文献

两栖动物皮肤分泌物中的抗菌肽具有广谱抗菌活性,为开发新的抗菌药物提供了新的途径。本文报道了一种新的抗菌肽,命名为Phylloseptin-PBa,该肽属于抗菌肽家族,是从紫边叶蛙(Phyllomedusa baltea)皮肤分泌物中分离得到的。设计了与蛙皮肤肽受体编码cDNA的信号肽位点互补的简并引物,对蛙皮肤分泌物cDNA文库进行了扩增。随后,使用反相HPLC和MS/MS裂解分离并鉴定肽。合成的复制品被证明具有抗S.金黄色葡萄球菌E. coli和C.白色念珠菌的浓度分别为8、128和8 mg/L。此外,它对人癌细胞系H460、PC 3和U251 MG表现出抗增殖活性,但对正常人细胞系(HMEC)的活性较低。此外,进行溶血测定以评估叶节菌素-PBa的哺乳动物细胞毒性。该肽含有较大比例的α-螺旋结构域,这可能是其抗菌和抗癌活性的原因。
Antimicrobial peptides from amphibian skin secretion display remarkable broad-spectrum antimicrobial activity and are thus promising for the discovery of new antibiotics. In this study, we report a novel peptide belonging to the phylloseptin family of antimicrobial peptides, from the skin secretion of the purple-sided leaf frog, Phyllomedusa baltea, which was named Phylloseptin-PBa. Degenerate primers complementary to putative signal peptide sites of frog skin peptide precursor-encoding cDNAs were designed to interrogate a skin secretion-derived cDNA library from this frog. Subsequently, the peptide was isolated and identified using reverse phase HPLC and MS/MS fragmentation. The synthetic replicate was demonstrated to have activity against S. aureus, E. coli and C. albicans at concentrations of 8, 128 and 8 mg/L, respectively. In addition, it exhibited anti-proliferative activity against the human cancer cell lines, H460, PC3 and U251MG, but was less active against a normal human cell line (HMEC). Furthermore, a haemolysis assay was performed to assess mammalian cell cytotoxicity of Phylloseptin-PBa. This peptide contained a large proportion of α-helical domain, which may explain its antimicrobial and anticancer activities.