Interaction of alamethicin with ether-linked phospholipid bilayers:: Oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies
Interaction of alamethicin with ether-linked phospholipid bilayers:: Oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies
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DOI：
10.1529/biophysj.105.067678
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发表时间：
2005-10-01
影响因子：
3.4
通讯作者：
Straus, SK
中科院分区：
文献类型：
--
作者：
Dave, PC;Billington, E;Straus, SK
用定向圆二色谱、31P固体核磁共振和差示扫描量热法研究了抗菌肽Alamethicin在由1，2-O-二十六烷基甘油-3-磷胆碱(DHPC)组成的醚联磷脂双层膜中的排列。这些测量是作为丙氨西林浓度相对于脂质浓度的函数进行的，并将结果与文献中报道的酯连接磷脂双层的结果进行比较。在室温下，丙氨西林进入DHPC双层膜的疏水核心，但导致的脂质紊乱比酯连接的1-棕榈酰基，2-油酰基-2-甘油-3-磷脂酰胆碱(POPC)脂双层膜更严重。这种取向紊乱似乎依赖于脂类属性，如双分子层厚度。此外，研究结果还表明，在较高的多肽浓度下，阿维菌素可以插入双分子膜的疏水核心区，但对于DHPC和POPC采用不同的机制，即环状插入和桶状插入。
The arrangement of the antimicrobial peptide alamethicin was studied by oriented circular dichroism, 31 P solidstate NMR, and differential scanning calorimetry in ether- linked phospholipid bilayers composed of 1,2-O-dihexadecyl- sn-glycero3- phosphocholine ( DHPC). The measurements were performed as a function of alamethicin concentration relative to the lipid concentration, and results were compared to those reported in the literature for ester-linked phospholipid bilayers. At ambient temperature, alamethicin incorporates into the hydrophobic core of DHPC bilayers but results in more lipid disorder than observed for ester-linked 1-palmitoyl, 2-oleoyl-sn-glycero-3-phosphatidylcholine ( POPC) lipid bilayers. This orientational disorder appears to depend on lipid properties such as bilayer thickness. Moreover, the results suggest that alamethicin inserts into the hydrophobic core of the bilayers ( at high peptide concentration) for both ether- and ester-linked lipids but using a different mechanism, namely toroidal for DHPC and barrel-stave for POPC.