Goraya J, Knoop F C, Conlon J M
Department of Biomedical Sciences, Creighton University Medical School, Omaha, Nebraska 68178, USA.
Peptides. 1999;20(2):159-63. doi: 10.1016/s0196-9781(98)00174-0.
A peptide, termed ranatuerin 1T, with growth-inhibiting activity toward Staphylococcus aureus, was isolated from an extract of the skin of the European brown frog, Rana temporaria. The primary structure of the peptide was established as: GLLSGLKKVG10 KHVAKNVAVS20LMDSLKCKIS30GDC. In common with other anti-microbial peptides from Ranid frogs, (e.g., ranalexin, ranatuerins, gaegurins, brevinins, esculetins, rugosins), ranatuerin IT contains an intramolecular disulfide bridge forming a heptapeptide ring but there is little structural similarity outside this cyclic region. The minimum inhibitory concentration (MIC) of ranatuerin 1T was 120 microM against the Gram-positive bacterium S. aureus and 40 microM against the Gram-negative bacterium Escherichia coli, but the peptide was not active against the yeast Candida albicans.
从欧洲棕蛙(林蛙)的皮肤提取物中分离出一种对金黄色葡萄球菌具有生长抑制活性的肽,称为林蛙抗菌肽1T。该肽的一级结构确定为:GLLSGLKKVG10 KHVAKNVAVS20LMDSLKCKIS30GDC。与来自蛙科青蛙的其他抗菌肽(如蛙皮素、林蛙抗菌肽、盖古林、短杆菌肽、七叶亭、皱皮蛙素)一样,林蛙抗菌肽1T含有一个形成七肽环的分子内二硫键,但在这个环状区域之外几乎没有结构相似性。林蛙抗菌肽1T对革兰氏阳性菌金黄色葡萄球菌的最低抑菌浓度(MIC)为120微摩尔,对革兰氏阴性菌大肠杆菌的最低抑菌浓度为40微摩尔,但该肽对白色念珠菌无活性。