Istituto Pasteur-Fondazione Cenci Bolognetti, La Sapienza University of Rome, 00185, Rome, Italy,
Cell Mol Life Sci. 2011 Jul;68(13):2267-80. doi: 10.1007/s00018-011-0718-2. Epub 2011 May 15.
Due to the rapid emergence of resistant microbes to the currently available antibiotics, cationic antimicrobial peptides have attracted considerable interest as a possible new generation of anti-infective compounds. However, low cost development for therapeutic or industrial purposes requires, among other properties, that the peptides will be small and with simple structure. Therefore, considerable research has been devoted to optimizing peptide length combined with a simple design. This review focuses on the similarities and differences in the mode of action and target cell specificity of two families of small peptides: the naturally occurring temporins from the skin of amphibia and the engineered ultrashort lipopeptides. We will also discuss the finding that acylation of cationic peptides results in molecules with a more potent spectrum of activity and a higher resistance to proteolytic degradation. Conjugation of fatty acids to linear native peptide sequences is a powerful strategy to engineer novel successful anti-infective drugs.
由于目前可用的抗生素迅速出现耐药微生物，阳离子抗菌肽作为新一代抗感染化合物引起了相当大的关注。然而，为了治疗或工业目的进行低成本开发，除其他特性外，肽还必须具有小尺寸和简单的结构。因此，人们投入了大量的研究来优化肽的长度，同时保持简单的设计。本综述重点介绍了两种小肽家族的作用模式和靶细胞特异性的异同：来自两栖动物皮肤的天然临时肽和工程超短脂肽。我们还将讨论酰化阳离子肽导致具有更有效谱的分子和更高的抗蛋白水解降解的发现。脂肪酸与线性天然肽序列的缀合是设计新型成功抗感染药物的有效策略。
