Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
Lipid reorganization induced by membrane-active peptides probed using differential scanning calorimetry
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DOI：
10.1016/j.bbamem.2009.05.001
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发表时间：
2009-09-01
影响因子：
3.4
通讯作者：
Alves, Isabel D.
中科院分区：
文献类型：
--
作者：
Joanne, Pierre;Galanth, Cecile;Alves, Isabel D.
一些细胞穿透肽（CPPs）和抗菌肽（AMPs）之间的生物学行为的重叠表明了共同的和不同的膜相互作用机制。因此，我们探索的能力，选定的CPP和AMP重组的平面分布的二元脂质混合物的差示扫描量热法（DSC）。此外，进行膜完整性测定和圆二色性（CD）实验。选择属于皮抑菌肽超家族的两种CPP（Penetratin和RL 16）和AMP（Drs B2和C-末端截短的类似物[1-23]-Drs B2和两种增塑剂DRP-PBN 2和DRP-PD 36 KF）。在这里，我们探讨了头基电荷和酰基链组成（长度和不饱和度）的肽/脂质相互作用的影响，通过使用二元脂质混合物。在所有研究的脂质混合物中，所有肽均显示为α-螺旋，除了在两性离子脂质混合物存在下的两种CPP和[1-23]-Drs B2，其中它们相当非结构化。取决于脂质组成和肽序列，特别是在AMP的情况下观察到与脂质表面的简单结合而不影响脂质分布。观察到脂质的募集和分离，主要是对于CPPs，肽构象与其在脂质侧向组织中的作用之间没有明确的关系。尽管如此，在大多数情况下，在初始静电识别后的肽带电荷的氨基酸和脂质头基之间，具有最低相变温度的脂质被阳离子肽选择性地招募，而那些具有最高相变分离。因此，CPP和AMP的膜活性可能与它们与膜缺陷的优先相互作用有关，所述膜缺陷对应于具有显著流动性的区域。此外，由于原核生物和真核生物的不同膜组成，横向异质性可能受到阳离子肽的不同影响，导致摄取或/和抗微生物活性。(C)2009爱思唯尔有限公司版权所有。
The overlapping biological behaviors between some cell penetrating peptides (CPPs) and antimicrobial peptides (AMPs) suggest both common and different membrane interaction mechanisms. We thus explore the capacity of selected CPPs and AMPs to reorganize the planar distribution of binary lipid mixtures by means of differential scanning calorimetry (DSC). Additionally, membrane integrity assays and circular dichroism (CD) experiments were performed. Two CPPs (Penetratin and RL16) and AMPs belonging to the dermaseptin superfamily (Drs B2 and C-terminal truncated analog [1-23]-Drs B2 and two plasticins DRP-PBN2 and DRP-PD36KF) were selected. Herein we probed the impact of headgroup charges and acyl chain composition (length and unsaturation) on the peptide/lipid interaction by using binary lipid mixtures. All peptides were shown to be alpha-helical in all the lipid mixtures investigated, except for the two CPPs and [1-23]-Drs B2 in the presence of zwitterionic lipid mixtures where they were rather unstructured. Depending on the lipid composition and peptide sequence, simple binding to the lipid surface that occur without affecting the lipid distribution is observed in particular in the case of AMPs. Recruitments and segregation of lipids were observed, essentially for CPPs, without a clear relationship between peptide conformation and their effect in the lipid lateral organization. Nonetheless, in most cases after initial electrostatic recognition between the peptide charged amino acids and the lipid headgroups, the lipids with the lowest phase transition temperature were selectively recruited by cationic peptides while those with the highest phase transition were segregated. Membrane activities of CPPs and AMPs could be thus related to their preferential interactions with membrane defects that correspond to areas with marked fluidity. Moreover, due to the distinct membrane composition of prokaryotes and eukaryotes, lateral heterogeneity may be differently affected by cationic peptides leading to either uptake or/and antimicrobial activities. (C) 2009 Elsevier B.V. All rights reserved.