Kharenko E P
Antibiot Khimioter. 1994 Jul;39(7):15-9.
Peptide dKRFdLE showed in vitro stable activity against gram negative bacteria i.e. Escherichia coli and Pseudomonas fluorescens when grown on the minimum glucose-mineral medium. Substitutions of the N- and C-end amino acids in the molecule of the peptide decreased its antibiotic activity. Comparison of the amino acid sequences of the known peptides with antibiotic activity made it possible to conclude that the presence of the doublet of the basic amino acids at the N-end and the doublet of the hydrophobic amino acids in the peptide core is necessary for the antibiotic activity. Possible mechanisms of the antibiotic action of short peptides and the ways for the rational search of new peptide antibiotics are discussed.
肽dKRFdLE在最低葡萄糖-矿物质培养基上生长时，对革兰氏阴性菌即大肠杆菌和荧光假单胞菌显示出体外稳定活性。肽分子中N端和C端氨基酸的取代降低了其抗生素活性。将具有抗生素活性的已知肽的氨基酸序列进行比较，可以得出结论，N端碱性氨基酸双峰和肽核心中疏水性氨基酸双峰的存在是抗生素活性所必需的。文中讨论了短肽抗生素作用的可能机制以及合理寻找新肽抗生素的方法。
