Ulvatne H, Haukland H H, Olsvik O, Vorland L H
Department of Medical Microbiology, P.O. Box 56, University Hospital of Tromsø, N-9038 Tromsø, Norway.
FEBS Lett. 2001 Mar 9;492(1-2):62-5. doi: 10.1016/s0014-5793(01)02233-5.
Antimicrobial peptides have been extensively studied in order to elucidate their mode of action. Most of these peptides have been shown to exert a bactericidal effect on the cytoplasmic membrane of bacteria. Lactoferricin is an antimicrobial peptide with a net positive charge and an amphipatic structure. In this study we examine the effect of bovine lactoferricin (lactoferricin B; Lfcin B) on bacterial membranes. We show that Lfcin B neither lyses bacteria, nor causes a major leakage from liposomes. Lfcin B depolarizes the membrane of susceptible bacteria, and induces fusion of negatively charged liposomes. Hence, Lfcin B may have additional targets responsible for the antibacterial effect.
为了阐明抗菌肽的作用模式，人们对其进行了广泛研究。已表明这些肽中的大多数对细菌的细胞质膜具有杀菌作用。乳铁蛋白是一种带净正电荷且具有两亲结构的抗菌肽。在本研究中，我们检测了牛乳铁蛋白（乳铁蛋白B；Lfcin B）对细菌膜的影响。我们发现Lfcin B既不裂解细菌，也不会导致脂质体大量渗漏。Lfcin B使易感细菌的膜去极化，并诱导带负电荷的脂质体融合。因此，Lfcin B可能还有其他负责抗菌作用的靶点。
